Cloning of cDNA encoding human placental protein 12(PP12): binding protein for IGF I and somatomedin

Grundmann, U.; Nerlich, Claudia; Bohn, H.; Rein, Theo

doi:10.1093/nar/16.17.8711

Cited by 21 publications

(12 citation statements)

References 4 publications

(1 reference statement)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Both IGFs also bind to the IGF-IL receptor and cross-react with the insulin receptor with a 100 times lower affinity than insulin (Rechler and Nissley, 1985). The complete amino acid sequence of this 28 kd IGFBP-1 was deduced from cDNA clones of human placenta, decidua and HEPG2 origin (Brewer et al, 1988;Brinkman et al, 1988;Grundmann et al, 1988;Julkunen et al, 1988;Lee et al, 1988). The presence of binding proteins that bind > 99% of the IGFs present in serum inhibits IGF -insulin receptor interactions and protects the organism from hypoglycaemia (Froesch et al, 1985).…”

Section: Introductionmentioning

confidence: 99%

Cloning, sequence analysis and expression of a cDNA encoding a novel insulin-like growth factor binding protein (IGFBP-2).

et al. 1989

View full text Add to dashboard Cite

Insulin‐like growth factors bind with high affinity to specific binding proteins in extracellular fluids. To identify structural characteristics of IGF‐binding proteins that might define their physiological roles, we determined the complete primary structure of a novel human IGF‐binding protein (IGFBP‐2) from a cloned cDNA. The cDNA encodes a 328 amino acid IGF‐binding protein precursor which contains a 39‐residue signal peptide. The mature 289 amino acid IGFBP‐2 has a predicted Mr of 31,325. Chinese hamster ovary (CHO) cells stably transformed with the IGFBP‐2 cDNA secreted a 36 kd protein which bound, with different affinities, IGFII and IGFI, but did not bind insulin. The predicted protein sequence of this IGF‐binding protein shares extensive amino acid homology (greater than 85%) with the IGF‐binding protein secreted by rat BRL‐3A cells, but less than 40% homology with human IGFBP‐1. Therefore IGFBP‐2, and not IGFBP‐1 as previously suggested, represents the human homologue of the rat BRL‐BP (alpha IGFBP‐2). Moreover, from alignment of the predicted protein sequences of IGFBP‐1 and IGFBP‐2, extensive conservation of the distribution of cysteine residues is observed. Although the overall amino acid homology shared by these proteins is not high, we suggest that they represent a family of structurally related human IGFBPs. Southern blot analysis of human DNA demonstrates that IGFBP‐2 is encoded by a single‐copy gene, different from that of IGFBP‐1.

show abstract

Section: Introductionmentioning

confidence: 99%

Cloning, sequence analysis and expression of a cDNA encoding a novel insulin-like growth factor binding protein (IGFBP-2).

et al. 1989

View full text Add to dashboard Cite

show abstract

“…Although sequence identities extend through the entire length of the protein, highest sequence conservation occurs between residues in the second cysteine repeat (EGP amino acids 91-130) and in the hydrophobic transmembrane domain. Furthermore, EGP shows sequence similarity to nidogen (27), a cell matrix protein, and placental protein 12, an IGF-I-binding protein secreted by the placenta (28,29). EGP shares with these proteins a similar pattern of cysteine repeats (Fig.…”

mentioning

confidence: 96%

“…EGP is also homologous to placental protein 12, which is secreted by the endometrium into the amniotic fluid during the first trimester-of pregnancy (28,32,33). Interestingly, many types of tumors express high levels of placental protein 12 (34,35).…”

mentioning

confidence: 99%

Epithelial glycoprotein is a member of a family of epithelial cell surface antigens homologous to nidogen, a matrix adhesion protein.

Simon

Podolsky

Moldenhauer

et al. 1990

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

The cell surface antigen, epithelial glycoprotein, defined by the monoclonal antibody HEA 125, is expressed on virtually all epithelial cell membranes but not on mesodermal or neural cell membranes. The cDNA encoding epithelial glycoprotein was isolated by HEA 125 antibody enrichment ofcolon tumor cDNA expressed transiently in COS cells. The sequence of the epithelial glycoprotein antigen is identical to the cell membrane protein recognized by the monoclonal antibody KS 1/4 and is homologous to the tumor-assoiated antigen GA733.These proteins share sequence homology to nidogen, an extracellular matrix component that appears to participate in cellmatrix adhesion. These proteins also share a homologous domain found in the Bi chain of laminin, a matrix adhesion protein, and placental protein 12, an insuidn-like growth factor I binding protein secreted during pregnancy that has been implicated in regulation of fetal growth. This common domain is also repeated multiple times within the thyroglobulin precursor. These fin gs suggest epithelial glycoprotein is a cell surface molecule involved in cell-cell or cell-matrix interaction.

show abstract

“…To begin to understand the process of liver regeneration, we used subtraction and differential screening analyses of cDNA libraries derived from regenerating rat liver to isolate many novel immediate-early genes (31). We found that one of the most abundant liver-specific early genes in regenerating liver encodes the rat homolog of the low-molecularweight insulinlike growth factor (IGF)-binding protein (8,10,21,24,29) (IGFBP-1), a protein that has been implicated in enhancing the IGF response (15,16,18).…”

mentioning

confidence: 99%

The gene encoding rat insulinlike growth factor-binding protein 1 is rapidly and highly induced in regenerating liver.

Mohn¹,

Melby²,

Tewari³

et al. 1991

Mol. Cell. Biol.

129

108

View full text Add to dashboard Cite

The liver is an epithelioid organ that can regenerate following partial hepatectomy. Although it is composed mainly of hepatocytes, it has a complex, multicellular architecture, implying that intercellular communications must exist during regeneration. As in other mitogen-stimulated cells, immediate-early growth response genes induced in the absence of prior protein synthesis are likely to play an important regulatory role in the regenerative process. Through differential screening of regenerating liver cDNA libraries, we found that one of the most highly expressed immediate-early genes in liver regeneration encodes the rat homolog of the low-molecular-weight insulinlike growth factor (IGF)-binding protein (IGFBP-1). This protein has been implicated in enhancing the mitogenic effect of IGF on tissues. IGFBP-1 gene induction is transcriptionally mediated and specific to regenerating liver, as the gene is not expressed in mitogen-stimulated fibroblasts. IGFBP-1 expression has been shown to increase under low-insulin conditions such as diabetes, and the complex regulation of expression is indicated by our finding that insulin treatment of H35 rat hepatoma cells, which induces proliferation, also causes a rapid decrease in transcription and expression of the IGFBP-1 gene. Of note, IGFBP-1 mRNA is abundant in fetal rat liver, implying that it participates in normal liver growth and development. Although regenerating liver cells continue to produce IGF-I, we did not detect IGF-I receptor mRNA during the first 24 h after hepatectomy. However, some IGFBPs may act to enhance the activity of IGF-I independently of IGF-I receptors. Thus, IGF-1 and IGFBPs may interact with hepatocytes or nonparenchymal liver cells, through either IGF-I or novel receptors. In this way, IGFBP-I and IGF-I could act in a paracrine and/or autocrine fashion in maintaining normal liver architecture during regeneration.

show abstract

Cloning of cDNA encoding human placental protein 12(PP12): binding protein for IGF I and somatomedin

Cited by 21 publications

References 4 publications

Cloning, sequence analysis and expression of a cDNA encoding a novel insulin-like growth factor binding protein (IGFBP-2).

Cloning, sequence analysis and expression of a cDNA encoding a novel insulin-like growth factor binding protein (IGFBP-2).

Epithelial glycoprotein is a member of a family of epithelial cell surface antigens homologous to nidogen, a matrix adhesion protein.

The gene encoding rat insulinlike growth factor-binding protein 1 is rapidly and highly induced in regenerating liver.

Contact Info

Product

Resources

About