Isolation and characterization of a laminin-binding protein from rat and chick muscle.

A major laminin-binding protein (LBP), distinct from previously described LBPs, has been isolated from chick and rat skeletal muscle (Mr 56,000 and 66,000, respectively). The purified LBPs from the two species were shown to be related antigenically and to have similar NH2-terminal amino acid sequences and total amino acid compositions. Protein blots using laminin and laminin fragments provided evidence that this LBP interacts with the major heparin-binding domain, E3, of laminin. Studies on the association of this LBP with muscle membrane fractions and reconstituted lipid vesicles indicate that this protein can interact with lipid bilayers and has properties of a peripheral, not an integral membrane protein. These properties are consistent with its amino acid sequence, determined from cDNAs (Clegg et al., 1988). Examination by light and electron microscopy of the LBP antigen distribution in skeletal muscle indicated that the protein is localized primarily extracellularly, near the extracellular matrix and myotube plasmalemma. While a form of this LBP has been identified in heart muscle, it is present at low or undetectable levels in other tissues examined by immunocytochemistry indicating that it is probably a muscle-specific protein. As this protein is localized extracellularly and can bind to both membranes and laminin, it may mediate myotube interactions with the extracellular matrix.

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Amino acid sequence and distribution of mRNA encoding a major skeletal muscle laminin binding protein: an extracellular matrix-associated protein with an unusual COOH-terminal polyaspartate domain.

The Journal of Cell Biology ◽

10.1083/jcb.107.2.699 ◽

1988 ◽

Vol 107 (2) ◽

pp. 699-705 ◽

Cited By ~ 38

Author(s):

D O Clegg ◽

J C Helder ◽

B C Hann ◽

D E Hall ◽

L F Reichardt

Keyword(s):

Extracellular Matrix ◽

Amino Acid ◽

Membrane Protein ◽

Amino Acid Sequence ◽

Biochemical Characterization ◽

Muscle Protein ◽

Binding Protein ◽

Single Gene ◽

Laminin Binding Protein ◽

Laminin Binding

Two cDNAs encoding an abundant chicken muscle extracellular matrix (ECM)-associated laminin-binding protein (LBP) have been isolated and sequenced. The predicted primary amino acid sequence includes a probable signal peptide and a site for N-linked glycosylation, but lacks a hydrophobic segment long enough to span the membrane. The COOH terminus consists of an unusual repeat of 33 consecutive aspartate residues. Comparison with other sequences indicates that this protein is different from previously described LBPs and ECM receptors. RNA blot analysis of LBP gene expression showed that LBP mRNA was abundant in skeletal and heart muscle, but barely detectable in other tissues. Blots of chicken genomic DNA suggest that a single gene encodes this LBP. The amino acid sequence and mRNA distribution are consistent with the biochemical characterization described by Hall and co-workers (Hall, D. E., K. A. Frazer, B. C. Hahn, and L. F. Reichardt. 1988. J. Cell Biol. 107:687-697). These analyses indicate that LBP is an abundant ECM-associated muscle protein with an unusually high negative charge that interacts with both membranes and laminin, and has properties of a peripheral, not integral membrane protein. Taken together, our studies show that muscle LBP is a secreted, peripheral membrane protein with an unusual polyaspartate domain. Its laminin and membrane binding properties suggest that it may help mediate muscle cell interactions with the extracellular matrix. We propose the name "aspartactin" for this LBP.

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Calsequestrin, an intracellular calcium-binding protein of skeletal muscle sarcoplasmic reticulum, is homologous to aspartactin, a putative laminin-binding protein of the extracellular matrix

Biochemical and Biophysical Research Communications ◽

10.1016/0006-291x(90)90895-t ◽

1990 ◽

Vol 166 (2) ◽

pp. 898-903 ◽

Cited By ~ 13

Author(s):

Paul J. Yazaki ◽

Sergio Salvatori ◽

Roger A. Sabbadini ◽

A. Stephen Dahms

Keyword(s):

Skeletal Muscle ◽

Extracellular Matrix ◽

Sarcoplasmic Reticulum ◽

Intracellular Calcium ◽

Calcium Binding ◽

Binding Protein ◽

Calcium Binding Protein ◽

Laminin Binding Protein ◽

Laminin Binding

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Effect of 32/67 kDa laminin-binding protein antibody on mouse embryo implantation

Reproduction ◽

10.1530/reprod/119.1.137 ◽

2000 ◽

pp. 137-142 ◽

Cited By ~ 7

Author(s):

C Zhang ◽

E Duan ◽

Y Cao ◽

G Jiang ◽

G Zeng

Keyword(s):

Extracellular Matrix ◽

Mouse Embryo ◽

Binding Protein ◽

Embryo Implantation ◽

Continuous Section ◽

Rabbit Igg ◽

Laminin Binding Protein ◽

Ectoplacental Cone ◽

Laminin Binding

Mouse embryo implantation depends on the complex interaction between the embryo trophoblast cells and the uterine environment, which deposits an extracellular matrix with abundant amounts of laminin. Intrauterine injection and blastocyst or ectoplacental cone culture models were used to study the effect of 32/67 kDa laminin-binding protein antibody on mouse embryo implantation in vivo and in vitro. Intrauterine injection of 32/67 kDa laminin-binding protein antibody (0.4 mg in 1 ml Ham's F-10 medium, 5 microl per mouse) into the left uterine horns of mice (n = 22) on day 3 of pregnancy inhibited embryo implantation significantly (P < 0.001) compared with the contralateral horns that had been injected with normal rabbit IgG. A continuous section study on day 5 after injection showed that the embryos in the control uteri implanted normally and developed healthily, but there were no embryos or the remaining embryos had disintegrated in the uteri injected with 32/67 kDa laminin-binding protein antibody. Blastocysts or ectoplacental cones were cultured in media containing 32/67 kDa laminin-binding protein antibody (0.2 mg ml(-1)) on laminin-coated dishes with normal rabbit IgG at the same concentration as in the controls. The 32/67 kDa laminin-binding protein had no effect on blastocyst or ectoplacental cone attachment, but prohibited the blastocyst or ectoplacental cone outgrowth and primary or secondary trophoblast giant cell migration. These results indicate that 32/67 kDa laminin-binding protein antibody blocked mouse embryo implantation by preventing embryo trophoblast cell invasion and migration through the uterine decidual basement membrane-like extracellular matrix which has a high laminin content.

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Adult and fetal human mesangial cells interact with specific laminin domains

AJP Renal Physiology ◽

10.1152/ajprenal.1991.261.4.f688 ◽

1991 ◽

Vol 261 (4) ◽

pp. F688-F695

Author(s):

B. S. Weeks ◽

J. B. Kopp ◽

S. Horikoshi ◽

F. B. Cannon ◽

M. Garrett ◽

...

Keyword(s):

Extracellular Matrix ◽

Western Blot ◽

Blot Analysis ◽

Western Blot Analysis ◽

Mesangial Cell ◽

Mesangial Cells ◽

Cell Attachment ◽

Binding Protein ◽

Laminin Binding Protein ◽

Laminin Binding

Mesangial cells are centrally located pericytes in the renal glomerulus. They are surrounded by an extracellular matrix and directly contact the glomerular basement membrane in vivo. Because these interactions are critical for renal development and function, we have studied human mesangial cell interactions with laminin, a major adhesive component of basement membranes present in the extracellular matrix of the mesangium. Human fetal and adult mesangial cell attachment was stimulated by both laminin and the laminin-derived synthetic peptides YIGSR-NH2, CQAGTFALRGDNPQG-NH2, and CIKVAVS-NH2. Furthermore, mesangial cells spread on laminin as well as on both the RGD-containing and CIKVAVS peptides. When added in solution, all three peptides inhibited mesangial cell attachment to laminin, and the latter two peptides inhibited mesangial cell spreading on laminin. Laminin affinity column chromatography demonstrated several low-molecular-mass laminin-binding proteins ranging from between 35 and 42 kDa, which predominated in fetal mesangial cells, whereas a higher molecular mass laminin-binding protein of 65 kDa was predominant in adult mesangial cells. Western blot analysis with an anti-32-kDa laminin-binding protein antibody showed increased expression of both 31- and 42-kDa proteins in fetal mesangial cells when compared with the adult. The antisera to the 32-kDa laminin-binding protein also inhibited fetal mesangial spreading on the CIKVAVS peptide. Western blot analysis with an anti-67-kDa laminin-binding protein antibody revealed a 110-kDa protein in adult mesangial cells that was not present in fetal mesangial cells.(ABSTRACT TRUNCATED AT 250 WORDS)

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Membrane orientation of laminin binding protein. An extracellular matrix bridging molecule of Leishmania donovani

European Journal of Biochemistry ◽

10.1046/j.1432-1033.2003.03768.x ◽

2003 ◽

Vol 270 (18) ◽

pp. 3806-3813 ◽

Cited By ~ 4

Author(s):

Keya Bandyopadhyay ◽

Sudipan Karmakar ◽

Aruna Biswas ◽

Pijush K. Das

Keyword(s):

Extracellular Matrix ◽

Leishmania Donovani ◽

Binding Protein ◽

Membrane Orientation ◽

Laminin Binding Protein ◽

Laminin Binding

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Laminin-binding protein 120 from brain is closely related to the dystrophin-associated glycoprotein, dystroglycan, and binds with high affinity to the major heparin binding domain of laminin

Journal of Biological Chemistry ◽

10.1016/s0021-9258(18)82427-9 ◽

1993 ◽

Vol 268 (20) ◽

pp. 14972-14980

Author(s):

S.H. Gee ◽

R.W. Blacher ◽

P.J. Douville ◽

P.R. Provost ◽

P.D. Yurchenco ◽

...

Keyword(s):

Binding Protein ◽

Binding Domain ◽

Heparin Binding ◽

High Affinity ◽

Heparin Binding Domain ◽

Laminin Binding Protein ◽

Laminin Binding

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Purification and characterization of a uterine retinol-binding protein in the bitch

Biochemical Journal ◽

10.1042/bj3110407 ◽

1995 ◽

Vol 311 (2) ◽

pp. 407-415 ◽

Cited By ~ 9

Author(s):

W C Buhi ◽

I M Alvarez ◽

V M Shille ◽

M J Thatcher ◽

J P Harney ◽

...

Keyword(s):

Amino Acid ◽

Dna Sequences ◽

Binding Protein ◽

Amino Acid Content ◽

Amino Acid Sequences ◽

Retinol Binding Protein ◽

Total Amino Acid ◽

Major Protein ◽

Serum Retinol ◽

Two Dimensional Gel Electrophoresis

A major canine endometrial secreted protein (cP6, 23,000-M(r)) was purified by ion-exchange and gel-filtration chromatography and characterized by two-dimensional gel electrophoresis. Anti-[human retinol-binding protein (hRBP)] serum identified cP6 on immunoblot analysis and immunoprecipitated cP6 from culture medium. This major protein was also shown to bind [3H]retinol. N-terminal and internal amino acid sequences were determined and compared with previously identified protein, RNA, or DNA sequences. N-terminal analysis revealed that cP6 had high identity and similarity to serum retinol-binding proteins (RBPs), while internal sequence analysis showed a strong similarity to rat androgen-dependent epididymal protein and beta-lactoglobulins. Amino acid analysis, however, showed significant differences between these proteins and cP6 in both total amino acid content and certain selected amino acids. Immunohistochemical analysis showed staining for RBP only in the uterine luminal epithelium. These studies suggest that bitch endometrium secretes a family of proteins (cP6), some of which bind [3H]retinol, are immunologically related to the RBP family, and have N-terminal and internal sequences with a high similarity to RBP, beta-lactoglobulins and other members of the lipocalin family. This family of proteins may be important in early development for supplying retinol or derivatives to the developing embryo.

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