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PubMed1996

Selective loss of myelin-associated glycoprotein from myelin correlates with anti-MAG antibody titre in demyelinating paraproteinaemic polyneuropathy.

The IgM monoclonal autoantibodies of patients with demyelinating paraproteinaemic polyneuropathy recognize a carbohydrate structure present on both myelin-associated glycoprotein (MAG) and protein zero (P0). These autoantibodies are sufficient to cause the disease but the mechanism of demyelination remains unclear. We have analysed nerve biopsies from eight patients with polyneuropathy and anti-MAG antibodies by quantitative immunohistochemistry and find a concordant pattern of reduced expression of myelin markers with the loss of myelinated fibres. We report here novel features of this disease, in particular a selective lack of detectable MAG in a large proportion of myelinated-fibres containing P0, myelin basic protein (MBP) and periaxin. There is also an inverse correlation of the distribution of MAG in peripheral nerve myelin with the serum anti-MAG antibody titres but no correlation of these titres with the loss of myelinated fibres. Double immunofluorescence staining of paraproteinaemic polyneuropathy (PPN) nerves shows anti-MAG IgM deposited on the periphery of myelinated fibres associated with or lacking MAG staining. These data suggest that the binding of anti-MAG antibodies to MAG and/or other myelin component(s) results in MAG downregulation and may have an essential role in the molecular mechanisms leading to demyelination and partial regeneration in this disease.

Antibody Specificity↗

PubMed1992

Changes of cytosolic Ca2+ interfere with measurements of cytosolic Mg2+ using mag-fura-2.

In rat pancreatic and submandibular gland acini during exposure to carbachol, changes in the fluorescence emission intensity ratio (R) of acini loaded with mag-fura-2 resemble changes in cytosolic Ca2+ concentration (Ca2+i) in acini loaded with fura-2. Furthermore, changes of R depend on the presence of extracellular Ca2+ (Ca2+o) but are much less influenced by changes in extracellular Mg2+ (Mg2+o). To evaluate interference with measurement of cytosolic Mg2+ (Mg2+i) by changes in Ca2+i, we determined the dissociation constant (Kd) and Hill coefficient (NH) of the Ca(2+)-mag-fura-2 and Mg(2+)-mag-fura-2 complexes in standard solutions, in intact acini after loading with the acetoxymethyl ester of mag-fura-2 (mag-fura-2/AM), and in lysates derived from acini loaded with mag-fura-2/AM. The Kd of the Ca(2+)-mag-fura-2 complex in acini (determined with ionomycin) was 20.49 +/- 5.20 microM, and NH was 1.44 +/- 0.16 (n = 24). Kd of the Mg(2+)-mag-fura-2 complex in acini was 2.25 +/- 0.98 mM, and NH was 1.20 +/- 0.20 (n = 25). Mean Kd values were slightly lower in acinar lysates and in solutions of standard mag-fura-2. In acini from either gland, 1,2-bis(2-aminophenoxy)ethan-N,N,N',N'-tetraacetic acid (BAPTA) suppressed carbachol-induced Ca2+i transients. The R value in stimulated acini loaded with BAPTA and mag-fura-2 increased slightly when Mg2+o was increased from less than 10 nM to 1.2 mM, suggesting that Mg2+ influx contributes to the maintenance of Mg2+i during exposure to carbachol. Under these conditions, pancreatic acinar Mg2+i is 0.53 +/- 0.14 mM (n = 5).(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗

PubMed1994

Anti-MAG antibodies: major effects of antigen purity and antibody cross-reactivity on ELISA results and clinical correlation.

There is controversy regarding the relationship of polyneuropathy syndromes to the presence of serum antibody binding to myelin-associated glycoprotein (MAG). Using standard ELISA methodology, we identified 74 sera that appeared to have high titers of IgM binding to MAG and found that only 34% of these sera stained MAG using Western blot methodology. Follow-up studies showed that two factors greatly influence concordance between ELISA and Western blot testing for anti-MAG antibodies. Sera with high titers of binding to both MAG and histone H3 identified by ELISA rarely stain MAG on Western blot. In addition, sera analyzed by ELISA often bind to impurities in the semipure MAG that is frequently used in ELISA assays. Further purifications to separate MAG from other contaminants improved concordance between ELISA and Western blot results to 85% to 90% in a retrospective analysis, as well as in a prospective study of 49 additional sera. Patients with a polyneuropathy and serum IgM binding to MAG preparations by ELISA but not by Western blot methodology had several different clinical syndromes, including gait disorders and asymmetric motor neuropathies. Patients with IgM binding to MAG by both assay methods usually had a distal, sensory-motor, symmetric polyneuropathy with some features of demyelination on electrodiagnostic testing.

Adult↗

PubMed1989

Glomerular filtration and tubular secretion of MAG-3 in the rat kidney.

Technetium-99m mercaptoacetyltriglycine (MAG-3) has recently been introduced as a new radiopharmaceutical for dynamic renal scintigraphy. To elucidate the mechanism of renal excretion, micropuncture experiments were performed in rat kidneys for direct measurements of glomerular filtration and tubular secretory capacity. Fluid of Bowman space was collected from superficial glomeruli and analyzed for its contents of [99mTc]MAG-3, [125I]hippurate and [3H]inulin during constant infusion of these compounds. The ratio of activity of ultrafiltrate to that of arterial plasma was 0.23 for MAG-3, 0.68 for hippurate and 1.04 for inulin which demonstrates that the filtrated amount of MAG-3 is only 23% of that of inulin, presumably because of higher plasma protein binding which was also measured in vitro and found to be 80 +/- 1.5% for MAG-3 and 32 +/- 2% for [125I]hippurate. Proximal and distal tubules were also micropunctured and their tubular fluid as well as the final urine analyzed for the activity of hippurate and MAG-3. The tubular fluid to plasma ratio values along the nephron and in the final urine were all lower for MAG-3 than for hippurate, indicating a lower secretory capacity. From measurements of whole renal clearance, GFR and plasma protein binding the filtered amount of MAG-3 was 0.26 and of hippurate 0.87 ml/min.g kidney weight (p less than 0.001) and the secreted amount 2.01 and 2.38 ml/min.g kidney weight (p less than 0.05), respectively. We conclude that MAG-3 is predominantly excreted by tubular secretion and that the lower renal clearance of MAG-3 as compared with that of hippurate is a result both of a substantially decreased glomerular filtration and of a lower tubular secretion.

Animals↗

PubMed1995

A mucin-like glycoprotein identified by MAG (mouse ascites Golgi) antibodies. Menstrual cycle-dependent localization in human endometrium.

Human endometrial glands synthesize and secrete a high molecular weight mucin-like glycoprotein in a menstrual cycle-dependent fashion. A novel moiety within this Golgi-associated glycoprotein is strongly reactive with IgG antibodies in numerous murine ascites, and has been termed MAG (mouse ascites Golgi). Immunohistochemical staining of 201 endometrial biopsies revealed the following patterns: MAG first appeared in the Golgi on cycle day 5, peaked on day 15, was present on the surface of the luminal epithelium between days 17 and 19, and was no longer detectable after day 19. MAG was also present in cervical, prostate, seminal vesicle, and lacrimal glands, pancreatic acinar cells, gall bladder and bile duct epithelium, and certain cells of the salivary and sweat glands. Interestingly, only tissues from blood group A individuals exhibited this staining. As a common link among all these cell types is the expression of mucins, we speculated that the MAG epitope could be a mucin-associated blood group A-related epitope. This hypothesis was tested by absorption experiments with a variety of glycoconjugates and erythrocytes and by immunoblots of MAG-rich material. The absorption studies demonstrated that only type III porcine mucin (< 1% sialic acid) and blood type A or AB erythrocytes were able to absorb the anti-MAG antibody. Inasmuch as N-acetyl-galactosamine alone, the terminal blood group A carbohydrate, did not block MAG antibody binding, the MAG epitope appears to involve N-acetylgalactosamine plus other determinants. Immunoblots of endometrial extracts and saliva from blood type A individuals revealed MAG-reactive material with a molecular weight > 200 kd under reducing conditions. Because the MAG epitope appears on the endometrial surface during the purported implantation window, we speculate that mucin-like epitopes could play a role in the earliest apposition phases of conceptus-endometrial interaction.

ABO Blood-Group System↗

PubMed1997

Soluble myelin-associated glycoprotein (MAG) found in vivo inhibits axonal regeneration.

Myelin-associated glycoprotein (MAG) is a potent inhibitor of axonal regeneration when used as a substrate for growth. However, to be characterized definitively as inhibitory rather than nonpermissive, MAG must also inhibit axonal regeneration when presented in solution. Here, we show that soluble dMAG (extracellular domain only), released in abundance from myelin and found in vivo and chimeric MAG-Fc, can potently inhibit axonal regeneration. For both dMAG and MAG-Fc, inhibition is dose-dependent. If myelin-conditioned medium is immunodepleted of dMAG, or if a MAG antibody is included with MAG-Fc, inhibition is completely neutralized. Together with MAG's ability to induce growth cone collapse, these results demonstrate that MAG is an inhibitory molecule and not merely nonpermissive. The results also suggest that MAG binds to a specific receptor and initiates a signal transduction cascade to effect inhibition. Importantly, these results indicate that soluble dMAG detected in vivo could contribute to the lack of regeneration in the mammalian CNS after injury.

Animals↗

PubMed1984

Myelin-associated glycoprotein (MAG) distribution in human central nervous tissue studied immunocytochemically with monoclonal antibody.

Recent biochemical data show that myelin-associated glycoprotein (MAG) is the antigen for a monoclonal antibody found in sera of patients with IgM paraproteinemia and neuropathy (Braun et al. 1982). Immunoreactivity of this antibody with CNS has not been described. To study this, monoclonal anti-MAG was used in the avidin-biotin-peroxidase complex method (Hsu et al. 1981) to immunostain paraffin and epon sections of human CNS. Well characterized polyclonal MAG antiserum (Quarles et al. 1981) was employed in comparison tests. In paraffin sections of developing CNS, both monoclonal and polyclonal MAG antisera stained oligodendroglia and myelin. In adult CNS, periaxonal regions of myelin sheaths were immunostained in paraffin sections and semithin epon sections treated with monoclonal and polyclonal anti-MAG. In electron-microscopic experiments that included milder pretreatment of epon thin sections and more precise reaction product localization, entire thickness of myelin sheaths were immunostained. Thus, in electron micrographs, monoclonal and polyclonal anti-MAG immunoreactivity also have the same localization. In other electron-microscopic experiments, the same reaction product localization was observed with antiserum to myelin basic protein (MBP), a known constituent of compact myelin. Thus, results with this monoclonal anti-MAG provide important new evidence to support the localization of MAG in compact CNS myelin. Our data also suggest that monoclonal antibodies against MAG will be useful in studies of the pathogenesis of multiple sclerosis and other demyelinating diseases.

Antibodies, Monoclonal↗

PubMed1994

Affinity studies of human anti-MAG antibodies in neuropathy.

Human IgM anti-myelin associated glycoprotein (MAG) antibodies from patients with neuropathy bind to oligosaccharide determinants shared by MAG and several other glycoconjugates in peripheral nerve. The apparent affinities of human anti-MAG antibodies were determined by an ELISA system which measures free antibody concentration at equilibrium in solution. Intact MAG, which bears multiple antigenic oligosaccharides, and monovalent oligosaccharides generated by pronase digestion of MAG were used as antigen. The human antibodies bound to intact MAG with dissociation constants of between 2.5 x 10(-10) M and 2.1 x 10(-7) M, and to the monovalent oligosaccharides with up to 100-fold lower affinities. Reduction of the pentameric IgM to its monomeric counterpart reduced its affinity to intact MAG 5-fold, but its avidity for immobilized MAG was reduced 500-fold as determined by ELISA. These studies show that IgM Anti-MAG antibodies exhibit relatively low intrinsic affinities for the oligosaccharide antigen, but their affinities and avidities are significantly increased by the multivalent nature of the antibody-antigen interaction.

Animals↗

PubMed1992

Comparison of the N-linked oligosaccharide structures of the two major human myelin glycoproteins MAG and P0: assessment and relative occurrence of oligosaccharide structures by serial lectin affinity chromatography of 14C-glycopeptides.

The N-linked oligosaccharide structures of human myelin-associated glycoprotein (MAG) and P0 have been characterized by serial lectin affinity chromatography (SLAC) of 14C-glycopeptides. 14C-Glycopeptides were prepared from purified MAG derivative and P0 by extensive proteolytic digestion and N-14C-acetylation. Assuming that all the 14C-glycopeptides were radiolabelled to the same specific radioactivity, the relative occurrence of the oligosaccharide structures was correlated to the amount of incorporated radioactivity. Sixteen and 15 fractions were generated by SLAC of MAG and P0 14C-glycopeptides, respectively. Despite this tremendous structural heterogeneity, the oligosaccharide "fingerprints" of MAG and P0 obtained by SLAC displayed similarities: (a) of the three types of N-linked oligosaccharides, the complex type accounted for 80.4% and 94.9% of MAG and P0 radioactivity, respectively; (b) biantennary complex oligosaccharides were the major structures present on MAG and P0; (c) approximately 60% of MAG and P0 oligosaccharides possessed a bisecting N-acetylglucosamine residue; and (d) large amounts of oligosaccharides with an alpha(1-6)fucose residue were found in both MAG and P0 and, noticeably, approximately 25% of the tri- and/or tetraantennary and approximately 90% of the bisected biantennary oligosaccharides of both glycoproteins contained alpha(1-6)fucose residues in the core. This study demonstrates that MAG and P0, both belonging to the immunoglobulin superfamily, display structural similarities in their N-linked oligosaccharide contents.

Carbon Radioisotopes↗

PubMed1985

Anti-MAG antibody and antibody complexes: detection by radioimmunoassay.

A radioimmunoassay (RIA) for measuring isotype-specific antibodies to the myelin-associated glycoprotein (MAG) was developed using radiolabeled CNS MAG in a double-antibody precipitation system. Anti-MAG activity was detected by RIA only in patients with neuropathy and anti-MAG M proteins. Anti-MAG IgM or IgG antibodies were not detected in serum of patients with Guillain-Barré syndrome, chronic relapsing polyneuritis, or multiple sclerosis (MS). Some patients with anti-MAG IgM M proteins also had complexes of IgG or IgA bound to the M protein. In one patient, anti-CNS MAG activity was detected by RIA, but not by ELISA or immunoblot. Anti-MAG antibody activity in patients with neuropathy seems to be isotypically restricted, and there is no evidence for antibody reactivity to MAG in other demyelinating diseases.

Antibodies, Anti-Idiotypic↗

PubMed1989

Technetium-99m MAG-3 clearances after captopril in experimental renovascular hypertension.

Rats with one kidney clamped (2K1C), both kidneys clamped (2K2C), unilaterally nephrectomized with remaining kidney clamped (1K1C), and normals, were studied using 99mTc mercaptoacetyltriglycine ([ 99mTc]MAG-3) and 131I orthoiodohippurate ([131I]OIH). Clearances of [99mTc]MAG-3 and [131I]OIH were performed after constricted rats became hypertensive. Clearances were repeated after i.v. Captopril. Clearances of [99mTc]MAG-3 and [131I]OIH in normals didn't change significantly after Captopril. Clearances of [99mTc]MAG-3 and [131I]OIH decreased insignificantly after Captopril in the 2K2C model. in the 2K1C group, normal kidney clearance increased ([99mTc]MAG-3 p less than 0.01 and [131I]OIH p less than 0.025) and clamped kidney clearance decreased after inhibition ([99mTc]MAG-3, p less than 0.01, [131I]OIH p less than 0.02). Clearances increased in the 1K1C group after Captopril ([99mTc]MAG-3 p less than 0.0025 and [131I]OIH, p less than 0.001). The ratio of [99mTc]MAG-3 to [131I]OIH before Captopril was 0.81 and 0.84 after Captopril. Changes in renal function after Captopril depend on the model of renovascular hypertension and possibly the dose administered. Technetium-99m MAG-3 clearance parallels [131I]orthoiodohippurate in renovascular hypertension.

Animals↗

PubMed1999

Myelin-associated glycoprotein, MAG, selectively binds several neuronal proteins.

Myelin-associated glycoprotein (MAG) is a potent inhibitor of axonal regeneration and also, depending on the age and type of neuron, can promote axonal growth. In addition, MAG influences stability of both myelin and the axon in the intact, mature nervous system. The identity of the neuron/axonal MAG-binding receptor responsible for effecting these responses is not known. Here we show that a soluble, chimeric form of MAG, MAG-Fc, can bind to the neuronal cell body and neurites equally well, in a sialic acid-dependent manner. Importantly, MAG-Fc specifically precipitates a number of surface proteins from post-natal cerebellar, dorsal root ganglion (DRG) and PC12 neurons. These proteins are not precipitated by a control Fc-containing chimera and are not apparent when a MAG antibody is included in the precipitation mix as a competitive inhibitor. Based on molecular weight, two prominent proteins of 190 and 250 kD are precipitated from all three neuron types. The 190 kD protein is a sialoglycoprotein, since it is not apparent in the precipitate from neurons which have been desialylated. Other proteins are precipitated but are less abundant and are different for each type of neuron. One or more of these proteins is/are likely to be the functional MAG receptor.

Animals↗

PubMed1996

Anti-MAG and anti-SGPG antibodies in neuropathy.

We compared the binding of human antibodies from patients with neuropathy to the myelin-associated glycoprotein (MAG), to its cross-reactive glycolipid sulfoglucuronyl paragloboside (SGPG), and to sections of peripheral nerve. Titers were correlated with the clinical presentation and results of electrophysiological and pathological studies. Most patients had a predominantly sensory or sensorimotor demyelinating neuropathy and highly elevated antibodies to both MAG and SGPG, but 2 had highly elevated antibodies to MAG alone, and 1 to SGPG alone. Two patients had predominantly motor neuropathy and highly elevated antibodies to SGPG which reacted with MAG by Western blot but not by enzyme-linked immunosorbent assay. One patient had amyotrophic lateral sclerosis and antibodies to SGPG but not to MAG. These studies indicate that the neuropathic syndrome associated with anti-MAG or -SGPG antibodies are more heterogeneous than previously suspected, and that although most of the antibodies react with both MAG and SGPG, some may react with MAG or SGPG alone.

Aged↗

PubMed2004

Immunoglobulin (Ig) M antibody against myelin associated glycoprotein (MAG): A comparison of methods.

The presence of immunoglobulin (Ig)M antibody against myelin associated glycoprotein (MAG) has been associated with autoimmune demyelinating, sensorimotor neuropathies. Approximately 50% of patients with IgM paraproteinemia and associated peripheral neuropathy possess antibodies against MAG. These autoantibodies are thought to interfere with the process of myelination, myelin maintenance, or axon-Schwann cell interaction. The detection of these autoantibodies is useful to the clinician and is suggestive of active demyelination in a peripheral neuropathy. Our objective in this study was to compare the results obtained using three different methods (dual enzyme immunoassay [EIA], immunofluorescent antibody [IFA] and Western blot [WB]) for detecting IgM antibody against MAG in patients suspected of having autoimmune demyelinating neuropathies. Since the dual EIA utilized two different antigens, results from this assay were separated into two groups: MAG and sulfate-3-glucuronyl paragloboside (SGPG). When compared to WB (gold standard), percent agreement, sensitivity, and specificity for EIA and IFA are as follows: MAG EIA (68.3, 100.0, and 60.6); SGPG EIA (95.1, 100.0, and 93.9); and myelin IFA (97.6, 100.0, and 97.0). The authors conclude that the SGPG EIA and myelin IFA compared well with the standard WB method when detecting IgM antibody against MAG (100 kD). Many sera demonstrated reactivity on the MAG EIA that were negative by WB (100 kD glycoprotein). The authors recommend screening for MAG IgM in suspected patient sera by SGPG EIA or myelin IFA and utilizing these same methods to titer sera confirmed positive by WB.

Autoantibodies↗

PubMed2001

Terminal latency index in polyneuropathy with IgM paraproteinemia and anti-MAG antibody.

Criteria for the diagnosis of chronic inflammatory demyelinating polyneuropathy (CIDP) are met by the polyneuropathy associated with immunoglobulin M (IgM) paraproteinemia and anti-myelin-associated glycoprotein (MAG) antibody (MAG-CIDP). However, MAG-CIDP differs from other types of CIDP, mainly in its poorer response to treatment. The utility of terminal latency index (TLI) as an electrophysiological marker for MAG-CIDP has been debated. In this study we confirmed its diagnostic usefulness and evaluated TLI threshold values for motor nerves investigated in routine nerve conduction studies. Median, ulnar, peroneal, and tibial TLIs of 11 subjects with MAG-CIDP, 18 with CIDP, and 76 healthy controls were compared, and threshold values for MAG-CIDP evaluated as the lowest value with a likelihood ratio higher than 10. Mean TLI values and TLIs of all but the peroneal nerve were significantly lower in MAG-CIDP. Median nerve TLI of 0.26 and ulnar nerve TLI of 0.33 were identified as the threshold TLI values for MAG-CIDP.

Aged↗

PubMed2001

Mag-indo1 affinity for Ca(2+), compartmentalization and binding to proteins: the challenge of measuring Mg(2+) concentrations in living cells.

A physicochemical study of the Mag-indo1 binding to Ca(2+) in solution showed that: (i) the characteristic fluorescence spectra of Ca(2+)-bound and Mg(2+)-bound Mag-indo1 are identical; (ii) two successive equilibria occur for increasing Ca(2+) concentrations; and (iii) the value of the dissociation constant of the first one, as determined by using a probe dilution protocol, amounts to 780 nM. In order to investigate the fluorescence level of Mag-indo1 trapped in cell organelles, fluorescence spectra of Mag-indo1-loaded fibroblasts were recorded before and after a digitonin permeabilization. Their resolution into cation-bound, protein-bound, and free Mag-indo1 characteristic spectra allowed measurement of the fluorescence intensities of these species. The intensities emitted from whole cells were compared to those emitted from organelles (assumed to be endoplasmic reticulum according to a DiOC(6) loading). The cation-bound Mag-indo1 fluorescence resulted partially (20 to 50%) from the cytosol for 30% of the cells, and totally from compartments for 70% of the cells. We found a concentration value of 500 nM for compartmentalized Ca(2+) and concluded that the Mag-indo1 binding to Ca(2+) is likely to affect drastically the Mg(2+) concentration measurements in cells. Moreover, we showed that the amount variation of protein-bound Mag-indo1 also affects Mg(2+) measurements when using the two-wavelength ratio method.

3T3 Cells↗

PubMed1989

Dynamic renal scanning using 99mTc-MAG-3 in man.

99mTc-labelled mercapto-acetyltriglycine (MAG-3) has recently been proposed as an ortho-iodohippurate (OIH) substitute for dynamic renal imaging. Experience with MAG-3 is, however, still limited and its biokinetics are not completely known. Moreover, most of the published studies have used HPLC purified MAG-3 which is inpractical for routine clinical work. In this study a commercially available kit of MAG-3 which does not require high performance liquid chromatography (HPLC) is used in 10 normal subjects and 15 patients with renal disease. The results obtained lead to the following conclusions: a. MAG-3 provided in kit form is suitable for renal imaging and semiquantitative analysis in routine clinical settings. b. There are significant differences between renal handling of MAG-3 and OIH, but the dynamic studies obtained with MAG-3 can be interpreted with the same criteria used for OIH studies. c. More information on MAG-3 kinetics is needed before this new radiopharmaceutical can be considered as an OIH substitute for truly quantitative studies such as effective renal plasma flow determinations.

Adult↗

PubMed1989

The distribution of MAG in association with the axonal lesions of canine progressive axonopathy.

The distribution of myelin-associated glycoprotein (MAG) was examined by immunocytochemistry in the spinal cord, accessory cuneate nucleus and lumbar ventral nerve roots of dogs affected by progressive axonopathy. These areas were chosen because of the frequency of spheroids and the associated changes in the myelin sheath, including vacuolation, demyelination, remyelination and accumulation of a granular, amorphous material within the sheath. Normal animals demonstrated the expected distribution of MAG; periaxonal and associated with uncompacted membrane such as Schmidt-Lanterman incisures. The majority of early axonal spheroids were surrounded by a MAG-positive zone but in the larger swellings and longer duration cases this was sometimes absent in places even though the axon was associated with Schwann cell processes. Axons in vacuolated fibres were commonly surrounded by a single adaxonal process of Schwann cell and normal periaxonal space. This was immunoreactive for MAG but in situations where the process was incomplete or the space distorted, staining was absent. The granular material failed to stain for MAG. Distorted Schmidt-Lanterman incisures, a feature of the advanced disease, were strongly positive. In the CNS, spheroids without myelin sheaths or unassociated with oligodendroglial processes were negative for periaxonal MAG. The study confirms the localization of MAG at the periaxonal space. It also raises the question of how the distribution of periaxonal MAG is affected by axonal swelling with a consequent increase in axonal surface area.

Animals↗