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

Reproduction ◽  
2000 ◽  
pp. 137-142 ◽  
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.

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

Reproduction ◽  
2000 ◽  
Vol 119 (1) ◽  
pp. 137-142 ◽  
Author(s):  
C Zhang ◽  
E Duan ◽  
Y Cao ◽  
G Jiang ◽  
G Zeng
Keyword(s):  
Mouse Embryo ◽  
Binding Protein ◽  
Embryo Implantation ◽  
Laminin Binding Protein ◽  
Laminin Binding

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

1988 ◽  
Vol 107 (2) ◽  
pp. 687-697 ◽  
Author(s):  
D E Hall ◽  
K A Frazer ◽  
B C Hann ◽  
L F Reichardt
Keyword(s):  
Skeletal Muscle ◽  
Extracellular Matrix ◽  
Amino Acid ◽  
Binding Protein ◽  
Light And Electron Microscopy ◽  
Muscle Membrane ◽  
Total Amino Acid ◽  
Isolation And Characterization ◽  
Laminin Binding Protein ◽  
Laminin Binding

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.

scholarly journals Expression of extracellular matrix metalloproteinase inducer and matrix metalloproteinases during mouse embryonic development

Reproduction ◽  
2007 ◽  
Vol 133 (2) ◽  
pp. 405-414 ◽  
Author(s):  
Li Chen ◽  
Masaaki Nakai ◽  
Robert J Belton ◽  
Romana A Nowak
Keyword(s):  
Extracellular Matrix ◽  
Matrix Metalloproteinases ◽  
Matrix Metalloproteinase ◽  
Embryo Development ◽  
Mouse Embryo ◽  
Expression Profiles ◽  
Embryo Implantation ◽  
Rt Pcr ◽  
Extracellular Matrix Metalloproteinase Inducer

Mouse embryo implantation is a highly invasive and controlled process that involves remodeling and degradation of the extracellular matrix of the uterus. Matrix metalloproteinases (MMPs) are the main proteinases facilitating this process. Extracellular matrix metalloproteinase inducer (EMMPRIN) can stimulate the production of MMPs and is required for successful implantation in the mouse. The aims of the present study were to examine the expression profiles of mRNA and proteins for EMMPRIN and MMPs in the developing mouse embryo in vitro, and to study whether EMMPRIN protein induces the production of MMPs by mouse blastocysts. EMMPRIN mRNA, detected by RT-PCR, was present at all stages of embryo development from the one-cell to the blastocyst outgrowth. EMMPRIN protein, observed by confocal microscopy, was present on the cell surface at the same stages of development as was the mRNA. Of seven MMPs studied, murine collagenase-like A (Mcol-A), murine collagenase-like B (Mcol-B) and gelatinase A (MMP-2) mRNAs were detected only in blastocyst outgrowths by RT-PCR. Gelatinase B (MMP-9) mRNA was detected both in expanded blastocysts and blastocyst outgrowths. MMP-2 and -9 proteins were detected in the cytoplasm of outgrowing trophoblast cells. Collagenase-2 (MMP-8), collagenase-3 (MMP-13), or stromelysin-1 (MMP-3) mRNAs were not present at any stage of pre- or peri-implantation mouse embryo development. Quantitative RT-PCR analyses showed that recombinant EMMPRIN protein did not stimulate MMP-2 or -9 expression by mouse blastocyst outgrowths. These data suggest that EMMPRIN may regulate physiological functions other than MMP production by mouse embryos during implantation.

Adult and fetal human mesangial cells interact with specific laminin domains

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)

scholarly journals The Laminin-Binding Protein Lbp from Streptococcus pyogenes Is a Zinc Receptor

2009 ◽  
Vol 191 (18) ◽  
pp. 5814-5823 ◽  
Author(s):  
Christian Linke ◽  
Tom T. Caradoc-Davies ◽  
Paul G. Young ◽  
Thomas Proft ◽  
Edward N. Baker
Keyword(s):  
Streptococcus Pyogenes ◽  
Metal Binding ◽  
Matrix Protein ◽  
Binding Protein ◽  
Extracellular Matrix Protein ◽  
Sequence Alignments ◽  
Laminin Binding Protein ◽  
Laminin Binding

ABSTRACT The common pathogen Streptococcus pyogenes colonizes the human skin and tonsils and can invade underlying tissues. This requires the adhesion of S. pyogenes to host surface receptors mediated through adhesins. The laminin-binding protein Lbp has been suggested as an adhesin, specific for the human extracellular matrix protein laminin. Sequence alignments, however, indicate a relationship between Lbp and a family of bacterial metal-binding receptors. To further analyze the role of Lbp in S. pyogenes and its potential role in pathogenicity, Lbp has been crystallized, and its structure has been solved at a resolution of 2.45 Å (R = 0.186; R free = 0.251). Lbp has the typical metal-binding receptor fold, comprising two globular (β/α)4 domains connected by a helical backbone. The two domains enclose the metal-binding site, which contains a zinc ion. The interaction of Lbp with laminin was further investigated and shown to be specific in vitro. Localization studies with antibodies specific for Lbp show that the protein is attached to the membrane. The data suggest that Lbp is primarily a zinc-binding protein, and we suggest that its interaction with laminin in vivo may be mediated via zinc bound to laminin.

scholarly journals 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.

1988 ◽  
Vol 107 (2) ◽  
pp. 699-705 ◽  
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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