Immunogold and immunoblot studies on a cell surface protein found in primary mesenchyme cells and in the cortical secretory vesicles of the sea urchin egg

1987 ◽  
Vol 45 ◽  
pp. 832-833
Author(s):  
G.L. Decker ◽  
M.C. Valdizan
Keyword(s):  
Cell Surface ◽  
Sea Urchin ◽  
Surface Protein ◽  
Egg Cell ◽  
Secretory Vesicles ◽  
Cell Surface Protein ◽  
Surface Complexes ◽  
Mesenchyme Cells ◽  
Lowicryl K4m ◽  
Primary Mesenchyme Cells

A monoclonal antibody designated MAb 1223 has been used to show that primary mesenchyme cells of the sea urchin embryo express a 130-kDa cell surface protein that may be directly involved in Ca2+ uptake required for growth of skeletal spicules. Other studies from this laboratory have shown that the 1223 antigen, although in relatively low abundance, is also expressed on the cell surfaces of unfertilized eggs and on the majority of blastomeres formed prior to differentiation of the primary mesenchyme cells.We have studied the distribution of 1223 antigen in S. purpuratus eggs and embryos and in isolated egg cell surface complexes that contain the cortical secretory vesicles. Specimens were fixed in 1.0% paraformaldehyde and 1.0% glutaraldehyde and embedded in Lowicryl K4M as previously reported. Colloidal gold (8nm diameter) was prepared by the method of Mulpfordt.

Localization and expression of msp130, a primary mesenchyme lineage-specific cell surface protein in the sea urchin embryo

Development ◽  
1987 ◽  
Vol 101 (2) ◽  
pp. 255-265 ◽  
Author(s):  
J.A. Anstrom ◽  
J.E. Chin ◽  
D.S. Leaf ◽  
A.L. Parks ◽  
R.A. Raff
Keyword(s):  
Cell Surface ◽  
Sea Urchin ◽  
Sea Water ◽  
Surface Protein ◽  
Specific Cell ◽  
Cell Surface Protein ◽  
Sea Urchin Embryo ◽  
A Cell ◽  
Mesenchyme Cells ◽  
Primary Mesenchyme Cells

In this report, we use a monoclonal antibody (B2C2) and antibodies against a fusion protein (Leaf et al. 1987) to characterize msp130, a cell surface protein specific to the primary mesenchyme cells of the sea urchin embryo. This protein first appears on the surface of these cells upon ingression into the blastocoel. Immunoelectronmicroscopy shows that msp130 is present in the trans side of the Golgi apparatus and on the extracellular surface of primary mesenchyme cells. Four precursor proteins to msp130 are identified and we show that B2C2 recognizes only the mature form of msp130. We demonstrate that msp130 contains N-linked carbohydrate groups and that the B2C2 epitope is sensitive to endoglycosidase F digestion. Evidence that msp130 is apparently a sulphated glycoprotein is presented. The recognition of the B2C2 epitope of msp130 is disrupted when embryos are cultured in sulphate-free sea water. In addition, two-dimensional immunoblots show that msp130 is an acidic protein that becomes substantially less acidic in the absence of sulphate. We also show that two other independently derived monoclonal antibodies, IG8 (McClay et al. 1983; McClay, Matranga & Wessel, 1985) and 1223 (Carson et al. 1985), recognize msp130, and suggest this protein to be a major cell surface antigen of primary mesenchyme cells.

Developmental expression of a cell-surface protein involved in calcium uptake and skeleton formation in sea urchin embryos

1987 ◽  
Vol 122 (2) ◽  
pp. 320-331 ◽  
Author(s):  
Mary C. Farach ◽  
Maria Valdizan ◽  
Helen R. Park ◽  
Glenn L. Decker ◽  
William J. Lennarz
Keyword(s):  
Cell Surface ◽  
Sea Urchin ◽  
Calcium Uptake ◽  
Surface Protein ◽  
Developmental Expression ◽  
Cell Surface Protein ◽  
Sea Urchin Embryos ◽  
A Cell ◽  
Skeleton Formation

Antibodies to a fusion protein identify a cDNA clone encoding msp130, a primary mesenchyme-specific cell surface protein of the sea urchin embryo

1987 ◽  
Vol 121 (1) ◽  
pp. 29-40 ◽  
Author(s):  
David S. Leaf ◽  
John A. Anstrom ◽  
Jia E. Chin ◽  
Michael A. Harkey ◽  
Richard M. Showman ◽  
...  
Keyword(s):  
Cell Surface ◽  
Fusion Protein ◽  
Sea Urchin ◽  
Cdna Clone ◽  
Surface Protein ◽  
Specific Cell ◽  
Cell Surface Protein ◽  
Sea Urchin Embryo ◽  
Specific Cell Surface

Arylsulfatase exists as non-enzymatic cell surface protein in sea urchin embryos

1998 ◽  
Vol 280 (3) ◽  
pp. 220-230 ◽  
Author(s):  
Keiko Mitsunaga-Nakatsubo ◽  
Koji Akasaka ◽  
Yoshihiro Akimoto ◽  
Eiji Akiba ◽  
Takashi Kitajima ◽  
...  
Keyword(s):  
Cell Surface ◽  
Sea Urchin ◽  
Surface Protein ◽  
Cell Surface Protein ◽  
Sea Urchin Embryos

Cloning and sequencing of a cell surface protein-encoding gene conserved in sea urchin species

Gene ◽  
1994 ◽  
Vol 141 (2) ◽  
pp. 243-248 ◽  
Author(s):  
Marta Di Carlo ◽  
Salvatore Perriera ◽  
Giovanna Montana ◽  
Daniele Paolo Romancino ◽  
Stefano Reale
Keyword(s):  
Cell Surface ◽  
Sea Urchin ◽  
Surface Protein ◽  
Cell Surface Protein ◽  
Cloning And Sequencing ◽  
Protein Encoding ◽  
A Cell ◽  
Encoding Gene

scholarly journals A calcium-binding, asparagine-linked oligosaccharide is involved in skeleton formation in the sea urchin embryo.

1989 ◽  
Vol 109 (3) ◽  
pp. 1289-1299 ◽  
Author(s):  
M C Farach-Carson ◽  
D D Carson ◽  
J L Collier ◽  
W J Lennarz ◽  
H R Park ◽  
...  
Keyword(s):  
Sea Urchin ◽  
Calcium Binding ◽  
Divalent Cations ◽  
Surface Protein ◽  
Oligosaccharide Chain ◽  
Oligosaccharide Moiety ◽  
Mesenchyme Cells ◽  
Skeleton Formation ◽  
Primary Mesenchyme Cells

We have previously identified a 130-kD cell surface protein that is involved in calcium uptake and skeleton formation by gastrula stage embryos of the sea urchin Strongylocentrotus purpuratus (Carson et al., 1985. Cell. 41:639-648). A monoclonal antibody designated mAb 1223 specifically recognizes the 130-kD protein and inhibits Ca+2 uptake and growth of the CaCO3 spicules produced by embryonic primary mesenchyme cells cultured in vitro. In this report, we demonstrate that the epitope recognized by mAb 1223 is located on an anionic, asparagine-linked oligosaccharide chain on the 130-kD protein. Combined enzymatic and chemical treatments indicate that the 1223 oligosaccharide contains fucose and sialic acid that is likely to be O-acetylated. Moreover, we show that the oligosaccharide chain containing the 1223 epitope specifically binds divalent cations, including Ca+2. We propose that one function of this negatively charged oligosaccharide moiety on the surfaces of primary mesenchyme cells is to facilitate binding and sequestration of Ca+2 ions from the blastocoelic fluid before internalization and subsequent deposition into the growing CaCO3 skeleton.

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