IngredientesAcid alpha-glucosidase, also called acid maltase, is an enzyme that helps to break down glycogen in the lysosome. It is functionally similar to glycogen debranching enzyme, but is on a different chromosome, processed differently by the cell, and is located in the lysosome rather than the cytosol.
Glycogen storage disease type II is caused by a deficiency of acid α-1,4-glucosidase (GAA; acid maltase, EC 3.2.1.20/3), which is a key enzyme in hydrolyzation of lysosomal glycogen to glucose.
Lysosomal acid α-glucosidase (GAA; EC 3.2.1.3) is an exo-1,4- and -1,6-α-glucosidase that hydrolyzes glycogen to glucose. Common alternative names and synonyms used in the medical and scientific literature include:
In humans, acid alpha-glucosidase is encoded by the GAA gene. Errors in this gene cause glycogen storage disease type II (Pompe disease). This gene encodes lysosomal alpha-glucosidase, which is essential for the degradation of glycogen to glucose in lysosomes. Different forms of acid alpha-glucosidase are obtained by proteolytic processing.
The disease is caused by a mutation in the acid alpha-glucosidase gene on the long arm of chromosome 17 at 17q25.2–q25.3 (base pair 75,689,876 to 75,708,272).
The gene spans approximately 20 kb and contains 20 exons with the first exon being noncoding. The coding sequence of the putative catalytic site domain is interrupted in the middle by an intron of 101 bp. The promoter has features characteristic of a "housekeeping" gene. The GC content is high (80%) and distinct TATA and CCAAT motifs are lacking.
More than 200 mutations in the GAA gene have been identified in people with Pompe disease. Many of these mutations change one of the protein building blocks (amino acids) used to make acid alpha-glucosidase. Other mutations insert or delete genetic material in the GAA gene.
Acid maltase is a lysosomal enzyme, present in all tissues, that hydrolyzes maltose and other branches of glycogen to yield glucose. It has no function in maintaining blood glucose concentrations.
The GAA gene provides instructions for producing an enzyme called acid alpha-glucosidase (also known as acid maltase). This enzyme is active in lysosomes, which are structures that serve as recycling centers within cells. Lysosomes use digestive enzymes to break down complex molecules into simpler ones that can be used by cells. Acid alpha-glucosidase normally breaks down a complex sugar called glycogen into a simpler sugar called glucose. Glucose is the main energy source for most cells.
Like other mammalian lysosomal enzymes, GAA is synthesized in the cytosol and traverses the endoplasmic reticulum (ER) where it is glycosylated with N-linked, high-mannose-type carbohydrate. In the Golgi apparatus, the high-mannose carbohydrate is modified on lysosomal proteins by the addition of mannose-6-phosphate (M6P), which targets these proteins to the lysosome. The M6P-modified proteins are delivered to the lysosome via interaction with either of two M6P receptors.
Acid maltase itself is not available as a conventional dietary supplement in the commercial sense. The enzyme exists in three principal contexts relevant to this reference article:
Currently available treatment options consist of enzyme replacement therapy (ERT) with alglucosidase alfa (Myozyme™), a form of human acid alpha-glucosidase (GAA) produced by recombinant DNA technology in Chinese hamster ovary cells, or with avalglucosidase alfa-ngpt (Nexviazyme®).
The disease also goes by the name "Type II glycogen storage disease (GSDII)" or "Acid maltase deficiency." It is named after a Dutch pathologist, Johannes Cassianus Pompe, who described an autopsy of a 7-month-old girl diagnosed with "idiopathic myocardial hypertrophy" and generalized muscle weakness. Dr. Pompe provided an insight into the underlying biology of the disease — massive vacuolar glycogen storage in virtually all tissues. The same year, 1932, similar cases were described.
Johannes Cassianus Pompe (1901–1945) studied medicine in Utrecht and trained in Amsterdam as a pathologist. In 1932 he reported on his findings in a girl of 7 months, who had succumbed to extreme hypertrophy of the heart. Microscopical analysis showed accumulation of glycogen not only in the heart, but also in the liver, kidneys, and skeletal muscles. Pompe's life was cut short near the end of World War II, when he was arrested and eventually executed by the occupying forces.
Pompe described the accumulation of glycogen in muscle tissue in some cases of a previously unknown disorder. This accumulation was difficult to explain as the enzymes involved in the usual metabolism of glucose and glycogen were all present and functioning.
In 1954 the disease was classified as glycogen storage disease type II to reflect the abnormal metabolism of glycogen. However, at that time, the cause of the disease, the "vacuolar" nature of the storage, and the apparent normal molecular structure of the accumulated glycogen all remained a mystery. The connection between lysosomes, the enzyme defect, and Pompe disease was made much later, in 1963, by a Belgian biochemist Henri-Gery Hers. He discovered a new enzyme (maltase) that carried out the hydrolysis of glycogen to glucose at an acidic pH.
The basis for the disease remained a puzzle until Christian de Duve's discovery of lysosomes in 1955, for which he won the Nobel Prize in 1974. His co-worker Henri G. Hers realized in 1965 that the deficiency of a lysosomal enzyme (alpha-glucosidase) for the breakdown of glycogen could explain the symptoms of Pompe disease. This discovery led to establishing the concept of lysosomal storage diseases, of which 49 have been described to date.
Subsequent molecular characterization of the GAA gene and recognition of a broad phenotypic continuum from classic infantile-onset to late-onset disease transformed disease classification and diagnosis.
Acid α-glucosidase (GAA) deficiency (GSDII), or Pompe disease, is the only glycogen storage disease directly involving abnormal lysosomal metabolism. In addition to being a lysosomal storage disorder, Pompe disease is also considered a neuromuscular disease, a metabolic myopathy, and a glycogen storage disease (GSD).
GAA is synthesized as a 110-kDa precursor containing N-linked carbohydrates modified with mannose-6-phosphate groups. Following trafficking to the lysosome, presumably via the mannose-6-phosphate receptor, the 110-kDa precursor undergoes a series of complex proteolytic and N-glycan processing events, yielding major species of 76 and 70 kDa.
During detailed characterization of human placental and recombinant human GAA, the peptides released during proteolytic processing were found to remain tightly associated with the major species. The 76-kDa form (amino acids 122–782) of GAA is associated with peptides of 3.9 kDa (amino acids 78–113) and 19.4 kDa (amino acids 792–952). The 70-kDa form (amino acids 204–782) contains the 3.9- and 19.4-kDa peptide species as well as a 10.3-kDa species (amino acids 122–199).
GAA maturation increases its affinity for glycogen by 7–10 fold. The encoded protein has a molecular mass of 104,645 Da and starts with a signal peptide. A remarkable homology is observed between this soluble lysosomal alpha-glucosidase and the membrane-bound intestinal brush border sucrase-isomaltase enzyme complex.
Acid maltase, also called α-1,4-glucosidase, is a lysosomal enzyme not in the energy pathway of the cell, so its deficiency does not produce dynamic symptoms in muscle. Acid maltase hydrolyzes the α-1,4 bonds in glycogen.
Acid alpha-glucosidase (GAA) is a lysosomal enzyme that hydrolyzes the alpha 1-4 linkage in maltose and other linear oligosaccharides, including the outer branches of glycogen, thereby breaking down excess glycogen in the lysosome.
This enzyme catalyzes the lysosomal pathway of glycogen degradation, presumably used during normal turnover of cellular constituents. The major pathway of glycogen degradation, used for glucose-6-phosphate production, occurs in the cytosol and is catalyzed by phosphorylase. Thus, in Pompe disease, the largest accumulation of glycogen is apparent in lysosomal structures.
Recombinant GAA is delivered to lysosomes by the cation-independent mannose-6-phosphate (M6P) receptor (CI-MPR), also known as the mannose-6-phosphate receptor (M6PR), through receptor-mediated endocytosis at the plasma membrane. It then exerts its enzymatic effect in lysosomes by converting glycogen to glucose.
The activities of the intestinal maltases are also described as alpha-glucosidase because they all digest linear starch oligosaccharides to glucose. Maltases are members of a group of intestinal enzymes called Family GH13 (Glycoside hydrolase family 13) that are responsible for breaking apart the α-glucosidase linkages of complex carbohydrates into simple glucose molecules. Acid maltase (the lysosomal form) is distinct from these intestinal brush-border maltases: while the intestinal enzymes (e.g., maltase-glucoamylase encoded by MGAM, and sucrase-isomaltase encoded by SI) degrade dietary carbohydrates in the gut lumen, acid maltase exclusively handles glycogen catabolism within the lysosomal compartment of cells throughout the body.
Pompe disease, also known as glycogen storage disease type II (GSD II) or acid maltase deficiency (AMD), is a genetic disorder caused by a deficiency of the acid alpha-glucosidase (GAA) enzyme, due to recessive mutations in the GAA gene, which leads to accumulation of lysosomal glycogen, diffusely but primarily affecting the skeletal and cardiac muscle tissue.
Pompe disease has an autosomal recessive inheritance pattern. This means the defective gene is located on an autosome, and two faulty copies of the gene — one from each parent — are required to be born with the disorder. Children have a one in four chance of inheriting the disorder when both parents carry the defective gene, and although both parents carry one copy of the defective gene, they are usually unaffected.
Pompe disease can vary widely in the degree of enzyme deficiency, severity, and age of onset, and over 500 different mutations in the GAA gene have been identified, many of which cause disease symptoms of varying severity.
Pompe disease is a rare, autosomal recessive genetic disorder caused by the deficiency of lysosomal acid α-glucosidase (GAA), an enzyme that degrades glycogen. The resulting accumulation of glycogen in body tissues, especially cardiac and skeletal muscles, disrupts the architecture and function of affected cells, leading to a variety of symptoms, clinical decline, and ultimately death.
The enzyme deficiency results in accumulation of intracellular glycogen leading to progressive disruption of cellular function, particularly in the heart, skeletal muscles, and diaphragm.
The age at onset of clinical manifestations, rate of progression, and severity, including degree of organ and/or muscular (skeletal, respiratory, and cardiac) involvement, largely depends on the severity of the mutations and consequently on the residual enzyme activity.
The clinical spectrum ranges from fatal hypertrophic cardiomyopathy and skeletal muscle myopathy in infants to relatively attenuated forms, which manifest as a progressive myopathy without cardiac involvement.
Infantile-Onset Pompe Disease (IOPD): Infantile Pompe disease is the most severe, resulting from complete or near complete acid α-glucosidase deficiency, and presents with symptoms that include severe lack of muscle tone, weakness, enlarged liver and heart, and cardiomyopathy. The tongue may become enlarged and protrude, and swallowing may become difficult. Most affected children die from respiratory or cardiac complications before the age of two.
Patients with onset of symptoms in early infancy (infantile-onset Pompe disease, IOPD) typically exhibit rapidly progressive hypertrophic cardiomyopathy and marked muscle weakness. Most of them die within the first year of life from cardiac and/or respiratory failure.
Late-Onset Pompe Disease (LOPD): Late-onset Pompe disease can present at any age older than 12 months and is characterized by a lack of cardiac involvement and better short-term prognosis.
In the majority of cases of Pompe disease, onset of symptoms occurs after infancy, ranging widely from the first to sixth decade of life (late-onset Pompe disease, LOPD). Progression of the disease is relentless, and patients eventually progress to loss of ambulation and death due to respiratory failure.
A well-documented adult presentation was summarized in an early case series from the medical literature: five patients with adult-onset acid maltase deficiency were described. All patients had developed initial pelvic girdle symptoms late in the second or early in the third decade and some years later developed signs of respiratory insufficiency. Typically they were tall, had weak and wasted paraspinal and gluteal muscles with lower limb weakness. All were orthopnoeic with marked diaphragmatic weakness.
The estimated global incidence of Pompe disease is 1:40,000, with variations in incidence reported between different ethnic groups. However, newer newborn screening data are revising this estimate upward. Pompe disease has a predicted genetic prevalence of approximately 1:10,000–30,000 based on newborn screening data, but historically this ranged between 1:35,000 and 1:138,000, with a carrier frequency of 1:77.
The historical newborn screening data suggest that the incidence of Pompe disease was higher than the traditional estimate of 1 in 40,000 births. About 75% of these cases were LOPD and 25% IOPD.
The cornerstone of glycogen storage disease type II diagnosis is the measurement of lysosomal GAA enzyme activity. Modern diagnostic protocols favor minimally invasive methods to detect GAA activity, such as testing in dried blood spot (DBS) samples or leukocytes in liquid blood. These assays are sensitive and reliable, though they can be complicated by interference from maltase glucoamylase, another enzyme active at acidic pH that may mask GAA deficiency. To overcome this challenge, inhibitors (e.g., acarbose) selectively inhibit maltase glucoamylase, enhancing the specificity of the GAA test.
Acid α-glucosidase (acid maltase) is measured by monitoring glucose release from maltose or glycogen at acid pH, or by using 4-methylumbelliferyl α-glucoside as substrate and measuring the fluorescence of 4-methylumbelliferone released.
Histological findings, e.g., the presence of periodic acid-Schiff (PAS)-positive vacuolated lymphocytes and positive staining with acid phosphatase in a muscle biopsy observed under light microscopy, can also support a glycogen storage disease type II diagnosis.
To confirm the diagnosis, the enzyme is usually assayed in lymphocytes and/or muscle tissue, and sometimes in urine. The muscle biopsy shows large vacuoles with a high glycogen content (periodic acid–Schiff [PAS]-positive) and strong reactivity for acid phosphatase, identifying them as secondary lysosomes.
Another potential biomarker for glycogen storage diseases is urinary excretion of tetrasaccharide 6-α-D-glucopyranosyl-maltotriose, which is increased in IOPD and other various conditions associated with glycogen turnover and, therefore, is unspecific.
Biochemical abnormalities include increased level of serum creatine kinase (CK), a biomarker of muscle injury, and urinary hexose tetrasaccharide (Hex4), a biomarker of disease substrate.
In March 2015, Pompe disease was added to the Recommended Uniform Screening Panel (RUSP) and since then a number of states have added Pompe disease to their slate of diseases for their Newborn Screening (NBS) program.
After the Discretionary Advisory Committee on Heritable Disorders in Newborns and Children (DACHDNC) added Pompe disease to the Recommended Uniform Screening Panel (RUSP) in 2013, the spread of Pompe disease newborn screening increased. However, challenges remain, including sensitivity and specificity of the assays, management of pseudodeficiency, time and method to treat IOPD patients detected by screening, immunomodulation, and management of later-onset Pompe disease patients discovered by screening.
Diagnostics shifted from biopsy-centered evaluation to dried blood spot enzyme testing plus GAA genotyping, with newborn screening enabling presymptomatic identification and earlier intervention.
Pompe disease is caused by a deficiency in the activity of the lysosomal enzyme acid alpha-glucosidase (GAA), an enzyme that degrades lysosomal glycogen. As a result, glycogen accumulates in lysosomes of many types of cells but accumulates predominantly in skeletal muscle fibers. The process is progressive and finally destroys the muscle architecture and function.
Cardiomegaly and hypertrophic cardiomyopathy is usually identified in the first weeks of life and progresses to left ventricular outflow obstruction and diminished lung volume. Progressive deposition of glycogen results in conduction defects with shortening of the PR interval on EKG. In untreated infants, death commonly occurs in the first two years of life from cardiopulmonary insufficiency.
The currently available enzyme replacement therapy (ERT) proved to be successful in reversing cardiac but not skeletal muscle abnormalities.
LOPD is characterized by more slowly progressive symptoms, with initial weakness affecting the paraspinal and lower-limb muscles. Diaphragmatic weakness is a particularly prominent feature: typically, patients had weak and wasted paraspinal and gluteal muscles with lower limb weakness. All were orthopnoeic with marked diaphragmatic weakness.
Pompe disease is a rare, inherited, devastating condition that causes progressive weakness, cardiomyopathy, and neuromotor disease due to the accumulation of glycogen in striated and smooth muscle, as well as neurons.
Glycogen accumulates in the lysosomes of all cells in patients with Pompe disease. In particular, glycogen accumulation is most pronounced in lysosomes of cardiac and skeletal muscle, liver, and other tissues. Accumulated glycogen ultimately impairs muscle function.
Years of research into the structure, processing, and function of acid alpha-glucosidase led to the development and 2006 approval of alglucosidase alfa (recombinant human acid alpha-glucosidase, Myozyme®/Lumizyme®), an enzyme replacement therapy and the first approved treatment for Pompe disease. Alglucosidase alfa has been a lifesaving treatment for patients with infantile-onset Pompe disease and radically improved daily life for patients with late-onset Pompe disease; however, long-term experience with alglucosidase alfa unraveled key unmet needs in these populations. Despite treatment, Pompe disease continues to progress, especially from a skeletal muscle perspective, resulting in a multitude of functional limitations.
Alglucosidase alfa, administered by intravenous infusion every 2 weeks at a dose of 20 mg/kg body weight, is approved by the European Medicines Agency (EMA) and the United States Food and Drug Administration (US FDA) as ERT in individuals with Pompe disease of all ages.
After several clinical trials in patients with infantile-onset Pompe disease and small-scale experience in a few people with late-onset Pompe disease, a randomized, double-blind, placebo-controlled trial in 90 patients with late-onset Pompe disease was conducted between 2005 and 2007. This study showed that patients treated with alglucosidase alfa for 1.5 years improved significantly compared to patients who received placebo.
A systematic review and meta-analysis of ERT in infantile-onset Pompe disease reported the following: this first systematic review with meta-analysis to evaluate the effect of ERT on IOPD included a total of 15 studies containing data from 316 patients. Patients were followed for a mean time of 48.3 months, and the mean age of starting ERT was 6.3 months, ranging from 0.1 to 43.1. Among the outcomes evaluated for IOPD, a benefit for left ventricular mass, total systemic vascular resistance, and survival were seen in meta-analysis. Alglucosidase alfa appears to be safe in the studied population. Although the occurrence of adverse events related to treatment or infusion are frequent, they are, in most cases, mild and easily treatable.
In a large descriptive analysis of late-onset Pompe disease patients: twenty-two studies containing clinical data from 437 LOPD patients were analyzed. Overall, at least two-thirds of patients were stabilized or exhibited improvements in creatine kinase levels, and muscular and/or respiratory function following treatment with alglucosidase alfa. Enzyme replacement therapy was well tolerated; the majority of adverse events were mild or moderate infusion-related reactions. Alglucosidase alfa treatment offers an effective and well-tolerated treatment that attenuates the progression of LOPD in the majority of patients.
Myozyme (alglucosidase alfa), developed by Sanofi Genzyme, was approved by the FDA in 2006 for individuals with infantile-onset Pompe disease, and was later marketed as Lumizyme (alglucosidase alfa) for individuals with late-onset Pompe disease.
In August 2021, the US Food and Drug Administration granted accelerated marketing approval to avalglucosidase alfa (Nexviazyme®) for the treatment of people 1 year of age and older living with late-onset Pompe disease.
The COMET trial extension study provided 97-week efficacy data: participants treated with avalglucosidase alfa for up to 97 weeks maintained improvements in respiratory function, motor function, muscle strength, and health-related quality of life that began in the first 49 weeks of treatment. Furthermore, participants who switched to avalglucosidase alfa after 49 weeks of treatment with alglucosidase alfa maintained disease stability as assessed by these parameters. In both treatment groups, no new safety or immunogenicity-related concerns were observed. Data from the COMET trial support long-term maintenance of positive clinical outcomes for patients receiving avalglucosidase alfa treatment.
The FDA approved cipaglucosidase alfa-atga for the treatment of Pompe disease on September 28, 2023. This drug helps to treat Pompe disease by the breakdown of glycogen within lysosomes. Late-onset Pompe disease is characterized by a deficiency in alpha glucosidase, leading to the accumulation of glycogen within lysosomes and subsequent cellular dysfunction. Cipaglucosidase alfa's targeted approach involves the administration of the recombinant human GAA (rhGAA) enzyme, providing a therapeutic replacement for the deficient natural enzyme. This drug aims to restore the normal physiological function of lysosomes, thereby mitigating the impact of Pompe disease on affected individuals.
Recombinant enzymes can be co-administered with pharmacological chaperones which can induce or stabilize a proper conformation of the enzyme, to prevent or reduce degradation of the enzyme and/or its unfolding into an inactive form, either in vitro (for example, in storage prior to administration) or in vivo. In a clinical trial conducted in 13 subjects with Pompe disease (3 early onset/infantile and 10 late onset) at 4 treatment centers in Italy, 20 to 40 mg/kg alglucosidase alfa was administered alone and then co-administered with 4 doses of 80 mg miglustat.
There are significant unmet needs as it relates to clinical care and therapeutics in Pompe disease as well as in research. The currently available treatments lose effectiveness over the long run and do not have penetration into neuronal tissues and show inconsistent penetration in certain muscles. More definitive gene therapy and enzyme replacement strategies are currently in development and testing.
Neither of the newer ERT products was shown to be superior to the standard of care product, alglucosidase alfa. The long-term effectiveness of these newer forms of ERT is unclear.
Overall, clinical evidence for ERT in Pompe disease is moderate to strong for well-defined outcomes in infantile-onset disease (cardiac mass, survival) but more heterogeneous in late-onset disease, owing to the broad age range at presentation, variable residual enzyme activity, and limited trial sizes inherent to a rare disease. Evidence should be interpreted with these constraints in mind.
The recommended dosage regimen of alglucosidase alfa is 20 mg/kg body weight, administered every 2 weeks by intravenous (IV) infusion, although dosage can vary accordingly to each patient.
The ERT is provided intravenously, typically every two weeks, with infusion times lasting about four hours.
In one clinical trial context, 20 to 40 mg/kg alglucosidase alfa was administered alone and then co-administered with 4 doses of 80 mg miglustat in a multi-centre Italian study.
No oral dietary supplement dose forms exist for acid maltase (acid alpha-glucosidase) as of the date of this article. All clinically described dosages pertain strictly to intravenous pharmaceutical-grade recombinant enzyme preparations administered under medical supervision.
Approximately 25% of patients had infusion-associated reactions, and 88–96% developed antidrug antibodies, with no apparent negative impact on outcomes.
Allergic reactions, including anaphylaxis, have been reported with ERT. The majority of adverse events were mild or moderate infusion-related reactions.
Approximately 25% of patients had infusion-associated reactions, and 88–96% developed antidrug antibodies, with no apparent negative impact on outcomes. However, because the exact role of antibody formation in patients with late-onset Pompe disease is not yet fully understood, the results of long-term studies should be awaited before drawing any definite conclusions on this issue.
Participants are tested for anti-avalglucosidase alfa antibodies monthly during the first 6 months and thereafter every 3 months. Every time a participant tests seropositive for antidrug antibody (ADA), serum is also tested for neutralizing antibodies (NAbs) to avalglucosidase alfa including inhibition of enzyme activity and uptake.
Avalglucosidase alfa was generally well tolerated. Rates of treatment-emergent adverse events (TEAEs) (86% vs. 92%), potentially treatment-related TEAEs (45% vs. 49%), and severe TEAEs (12% vs. 14%) were broadly similar between avalglucosidase alfa and alglucosidase alfa. Serious TEAEs were reported in 16% and 25% of patients, respectively. Protocol-defined severe infusion-associated reactions were uncommon (0% vs. 4%, respectively).
Assays for acid maltase activity can be complicated by interference from maltase glucoamylase, another enzyme active at acidic pH that may mask GAA deficiency. To overcome this challenge, inhibitors such as acarbose selectively inhibit maltase glucoamylase, enhancing the specificity of the GAA test.
A phenomenon known as GAA pseudodeficiency — in which apparent enzyme activity is reduced but the individual is clinically unaffected — represents a notable diagnostic safety consideration. Another major challenge relating to diagnosis of Pompe disease is GAA pseudodeficiency.
Because ERT is required throughout life, most patients have a central line placed. Long-term intravenous access introduces independent infection and thrombosis risks associated with indwelling catheters, which are managed in specialist clinical settings.
The currently available enzyme replacement therapy (ERT) proved to be successful in reversing cardiac but not skeletal muscle abnormalities. Although the overall understanding of the disease has progressed, the pathophysiology of muscle damage remains poorly understood.
The current treatment for Pompe disease is enzyme replacement therapy using recombinant human alpha-glucosidase. Ongoing research aims to develop improved or new enzymes, as well as other treatments, such as gene therapy and substrate reduction strategies.
The muscle glycogen biosynthesis pathway is the focus of substrate reduction therapy for Pompe disease. RNA interference technology has been employed to impede the glycogen synthase (GYS1) muscle isoform. In GAA-knockout mice, this resulted in a significant reduction in the amount of lysosomal glycogen stored in myogenic cells and primary muscle cells. Significant reduction in glycogen storage and improvement in cardiomegaly, muscle atrophy, and exercise capacity opened new perspectives for treatment.
New therapeutic approaches, such as modified enzyme replacement therapies and gene editing, are essential for overcoming current limitations and improving treatment efficacy in Pompe disease.
Condiciones de salud que Maltasa ácida puede ayudar a apoyar.
Acid maltase (acid alpha-glucosidase) hydrolyzes glycogen within lysosomes as well as maltose in the gut, playing a role in carbohydrate digestion. Deficiency causes Pompe disease (glycogen storage disease type II). In the digestive enzyme supplement context, it is included in formulations to support glycogen and starch breakdown.
Sistemas corporales que Maltasa ácida puede ayudar a apoyar.
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