Amphiphysin, a novel protein associated with synaptic vesicles.

Lichte, Beate; Veh, Rüdiger W.; Meyer, Helmut E.; Kilimann, Manfred W.

doi:10.1002/j.1460-2075.1992.tb05317.x

Cited by 184 publications

(176 citation statements)

References 41 publications

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“…Its expression in mature synapses plausibly explains the staining of the neuropil noted throughout the mouse nervous system and is reminiscent of that seen with amphiphysin and CRMP5. 5,41,42 The widespread distribution of MAP1B throughout the central and peripheral nervous systems is consistent with the diverse and multifocal neurologic impairment observed with PCA-2 autoimmunity. 40 Amino acid sequence homologies of MAP1A and MAP1B (see Supplementary Table 1) would account for the reactivity of patient IgG with MAP1A protein in some cases.…”

Section: Discussionsupporting

confidence: 61%

Microtubule‐associated protein 1B: Novel paraneoplastic biomarker

Gadoth¹,

Kryzer²,

Fryer³

et al. 2017

Annals of Neurology

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Objective: To report the identification of microtubule-associated protein (MAP) 1B as the antigen of the previously described Purkinje cell cytoplasmic antibody type 2 (PCA-2) antibody, its frequency, and clinical, oncological, and serological associations. Methods: Archival serum or cerebrospinal fluid (CSF) specimens were available from 96 of 118 consecutive PCA-2-IgG-seropositive patients identified during 1993-2016. The autoantigen, defined in mouse brain lysate by Western blot and mass spectrometry, was confirmed by dual immunohistochemical staining using commercial antibodies. The major antigenic region was defined by Western blot using recombinant protein fragments. Results: IgG in 95 of 96 patients' serum or CSF (but in none of 98 healthy or disease control subjects' serum specimens) bound to recombinant MAP1B. A minority (17.5%) of patients' IgG also bound to MAP1A. PCA-2 was often accompanied by additional neural autoantibody markers of small-cell carcinoma, including collapsin responsemediated protein 5 (CRMP5) IgG (26%) or antineuronal nuclear antibody type 1 (ANNA-1) IgG (also known as antiHu; 13%). Neurological manifestations in 95 patients were (in decreasing frequency): peripheral neuropathy, 53%; cerebellar ataxia, dysmetria, or dysarthria, 38%; and encephalopathy, 27%. Cancer (majority small-cell lung carcinoma [SCLC]) was detected in 66 of 84 evaluated patients (79%). The MAP1B (PCA-2) autoantibody detection rate, among approximately 70,000 patients undergoing service neural autoantibody evaluation in 2015, was 0.024%, equaling amphiphysin IgG (0.026%) and more common than ANNA-2 (also known as anti-Ri; 0.016%) and PCA-Tr (also known as delta/notch-like epidermal growth factor-related receptor [DNER]; 0.006%). Interpretation: MAP1B, the PCA-2 autoantigen, represents a novel target in paraneoplastic neurological disorders and has high predictive value for SCLC. Its relatively high prevalence, compared with other recognized paraneoplastic neural autoantibodies, justifies its testing in comprehensive paraneoplastic neural autoantibody evaluation. ANN NEUROL 2017;81:266-277 I n 2000, Vernino and Lennon 1 reported 10 patients with neurological autoimmunity, 9 of whom had imaging or histopathologic evidence of lung cancer (8 biopsyproven small-cell lung carcinoma [SCLC]). Their serum IgG bound to a protein of 280kDa mass in both rodent brain and a SCLC line and yielded a characteristic staining pattern on rodent neural tissues. The autoantibody was named Purkinje cell cytoplasmic antibody type 2 (PCA-2), to distinguish it from a biomarker of ovarian and breast cancer-related cerebellar degeneration, PCA-1 (also known as anti-Yo). 2 The neurological associations initially reported for PCA-2 were mixed, of subacute onset and predominantly central (brainstem and limbic encephalitis, cerebellar ataxia), but some patients had peripheral manifestations (Lambert-Eaton myasthenic syndrome [LEMS] or autonomic or motor neuropathy). 1 Our study extends the immunochemical characteristization of PCA-2 IgG an...

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Section: Discussionsupporting

confidence: 61%

Microtubule‐associated protein 1B: Novel paraneoplastic biomarker

Gadoth¹,

Kryzer²,

Fryer³

et al. 2017

Annals of Neurology

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“…Synaptojanin Baculovirus Transfer Vector Constructs-A BamHIHindIII fragment from nucleotides 181 to 747, digested from a fulllength synaptojanin cDNA (clone 9) (6), was subcloned into the BamHIHindIII sites of pBluBac 4 (Invitrogen) (generating clone [1][2][3][4][5][6][7][8][9][10][11][12][13][14][15][16][17][18]. A 5Ј fragment encoding the N-terminal of synaptojanin with a His 6 tag was then generated by PCR with Vent Polymerase (New England Biolabs) using the forward oligonucleotide 5Ј-GCGGGATCCATGCATCACCAC-CACCACCACGCGTTCAGCAAGGATTTCG, which encodes a BamHI site, and the reverse oligonucleotide 5Ј-ATGCGGTCCTCATCTGAAG, which corresponds to clone 9 at nucleotide positions 470 -489.…”

Section: Methodsmentioning

confidence: 99%

“…Amphiphysin was first identified in chicken synaptic fractions (13) and mammalian amphiphysin, which is concentrated in presynaptic nerve terminals, has been implicated in synaptic vesicle endocytosis (14). A role for amphiphysin in endocytosis is supported by studies on its yeast homologues, RVS 161 and RVS 167 (15)(16)(17).…”

mentioning

confidence: 99%

Identification of the Major Synaptojanin-binding Proteins in Brain

Heuvel

Bell

Ramjaun

et al. 1997

Journal of Biological Chemistry

165

156

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Synaptojanin is a nerve-terminal enriched inositol 5-phosphatase thought to function in synaptic vesicle endocytosis, in part through interactions with the Src homology 3 domain of amphiphysin. We have used synaptojanin purified from Sf9 cells after baculovirus mediated expression in overlay assays to identify two major synaptojanin-binding proteins in rat brain. The first, at 125 kDa, is amphiphysin. The second, at 40 kDa, is the major synaptojanin-binding protein detected, is highly enriched in brain, is concentrated in a soluble synaptic fraction, and co-immunoprecipitates with synaptojanin. The 40-kDa protein does not bind to a synaptojanin construct lacking the proline-rich C terminus, suggesting that its interaction with synaptojanin is mediated through an Src homology 3 domain. The 40-kDa synaptojanin-binding protein was partially purified from rat brain cytosol through a three-step procedure involving ammonium sulfate precipitation, sucrose density gradient centrifugation, and DEAE ion-exchange chromatography. Peptide sequence analysis identified the 40-kDa protein as SH3P4, a member of a novel family of Src homology 3 domain-containing proteins. These data suggest an important role for SH3P4 in synaptic vesicle endocytosis.

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“…Four BAR protein-encoding genes have been identified in the mammalian system, namely, Amphiphysin I, Bin1 (also known as AmpII), Bin2, and Bin3 (Lichte et al, 1992;Sakamuro et al, 1996). All BAR genes encode protein products with a unique signature domain termed the BAR domain (Sakamuro et al, 1996).…”

Section: Bin1 and Its Different Isoformsmentioning

confidence: 99%

Cardiac BIN1 (cBIN1) is a regulator of cardiac contractile function and an emerging biomarker of heart muscle health

Zhou

Hong

2016

Sci. China Life Sci.

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In recent decades, a cardiomyocyte membrane scaffolding protein bridging integrator 1 (BIN1) has emerged as a critical multifunctional regulator of transverse-tubule (t-tubule) function and calcium signaling in cardiomyocytes. Encoded by a single gene with 20 exons that are alternatively spliced, more than ten BIN1 protein isoforms are expressed with tissue and disease specificity. The recently discovered cardiac alternatively spliced isoform BIN1 (cBIN1 or BIN1+13+17)plays a crucial role in organizing membrane microfolds within cardiac t-tubules. These cBIN1-induced microfolds form functional dyad microdomains by trafficking L-type calcium channels (LTCC) to t-tubule membrane and recruiting ryanodine receptors (RyR) to junctional sarcoplasmic reticulum membrane. When cBIN1 is transcriptionally reduced as occurs in heart failure, cBIN1-microfolds are disrupted and fail to form LTCC and RyR couplons. As a result, impaired dyad formation limits excitation-contraction coupling thus cardiac contractility, and accumulation of orphaned leaky RyRs outside of dyads increases ventricular arrhythmias. Reduced myocardial BIN1 in heart failure is also detectable at the blood level, and plasma BIN1 level predicts heart failure progression and future arrhythmias in cardiomyopathy patients. Here we will review the recent progress in BIN1-related cardiomyocyte biology studies and discuss the diagnostic and predictive values of cBIN1 in future clinical use. heart failure, cBIN1, t-tubules, calcium transient, arrhythmias Citation:Zhou, K., and Hong, T. (2017). Cardiac BIN1 (cBIN1) is a regulator of cardiac contractile function and an emerging biomarker of heart muscle health.

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Amphiphysin, a novel protein associated with synaptic vesicles.

Cited by 184 publications

References 41 publications

Microtubule‐associated protein 1B: Novel paraneoplastic biomarker

Microtubule‐associated protein 1B: Novel paraneoplastic biomarker

Identification of the Major Synaptojanin-binding Proteins in Brain

Cardiac BIN1 (cBIN1) is a regulator of cardiac contractile function and an emerging biomarker of heart muscle health

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