Amino-terminal sequences of a novel heparin-binding protein from human, bovine, rat, and chick brain: High interspecies homology

Huber, Daniel; Gautschi-Sova, Peter; Bőhlen, Peter

doi:10.1007/bf00969930

Cited by 25 publications

(7 citation statements)

References 19 publications

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“…Although not all of the multiple forms of pPTN were individually characterized, their reactivity with anti-PTN(l-14) antiserum suggests that the N-termini of these proteins were intact. Previously it was shown that bovine brain-derived PTN was purified as (Milner et al 1989, Rauvala 1989, Huber et al 1990 ). bcDNA analysis predicts a Cys residue at positions 15 and 23 (Kovesdi et al 1990, Li et al 1990, Merenmies & Rauvala 1990).…”

Section: Discussionmentioning

confidence: 99%

“…Although the mitogenic activity of PTN has been the subject of some controversy (Huber et al 1990, Fang et al 1992, Milner et al 1992, evidence that this factor plays a role in cell growth regulation was shown by the acquisition of a transformed phenotype by NIH 3T3 cells and SW-13 human adrenal carcinoma cells after transfection with PTN cDNA (Fang et al 1992, Chauhan et al 1993). In addition, high levels of PTN mRNA have been detected in a variety of tumours (Fang et al 1992, Tsutsui et al 1993.…”

Section: Introductionmentioning

confidence: 98%

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Pig uterine luminal fluid contains the developmentally regulated neurotrophic factor, pleiotrophin

Brigstock

Kim²,

Steffen³

1996

Journal of Endocrinology

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The pig conceptus produces a non-invasive placenta which is probably dependent on uterine secretory products during both the pre- and post-attachment periods. Since some of these factors are also produced during the oestrous cycle, uterine luminal flushings (ULF) from adult nonpregnant pigs were analysed to identify potentially important maternally-secreted growth factors or cytokines. ULF contained several proteins that were detected on Western blots by an antibody raised against the N-terminal 14 amino acids of rat pleiotrophin (PTN). One of the proteins co-migrated on SDS-PAGE gels and co-eluted from heparin-affinity columns with 18 kDa recombinant human PTN, suggesting its identity as the intact native porcine PTN (pPTN) molecule. Additional immunoreactive forms of pPTN were identified that were of lower molecular mass (14-16 kDa), had lower heparin-affinities, were more hydrophobic, and were apparently C-terminally truncated. Native pPTN was isolated from ULF using cation-exchange chromatography, heparin-affinity fast protein liquid chromatography and C4 reverse-phase high performance liquid chromatography. Structural analysis of the purified protein resulted in definitive identification of 15 out of 17 N-terminal amino acids; these were 100% conserved with the corresponding residues of human, bovine and rat PTN. These results demonstrate various biochemical properties of pPTN and suggest that, in addition to the apparent involvement of PTN in differentiation during early neonatal life, it may be delivered in uterine secretory fluids to, as yet, undefined target cells in the reproductive tract of the adult female.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 98%

Pig uterine luminal fluid contains the developmentally regulated neurotrophic factor, pleiotrophin

Brigstock

Kim²,

Steffen³

1996

Journal of Endocrinology

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“…The extent of similarity between the coding sequences is quite low for the same protein from different species; for humadmurine, 87.7% [7] ; for chickedmamnmal, 73%. In contrast, HBGAM has more than 99% similarity between rat and human [26] and 94% similarity between chicken and rat. [27].…”

Section: General Organisation Of the Rihb Genementioning

confidence: 93%

Organisation and Promoter Activity of the Retinoic‐acid‐induced‐heparin‐binding (RIHB) Gene

Duprez

Treagger

Pecqueur

et al. 1994

European Journal of Biochemistry

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The heparin-binding protein, RIHB, is encoded by a gene that is expressed temporarily during the early period of chicken embryogenesis. We have now isolated genornic clones of the chicken RIHB gene, determined its transcription initiation sites, characterized its promoter region and established the functional activity of the RIHB gene promoter. The 5' flanking region and the beginning of the first exon revealed a structural organisation characteristic of housekeeping and growth-control-related genes. It lacked canonical TATA or CAAT boxes but contained several GC boxes. The structure of the RIHB gene is compared with those of the human and mouse midgestation kidney (MK) genes. In the coding exons, the similarities between the three genes are striking. In contrast, the structure and location of the first non-coding exon is different. Analysis of the promoter activity suggests an indirect regulation of transcription by retinoic acid and demonstrates a high degree of complexity of the regulation of the RIHB gene.We have previously purified to homogeneity a secreted heparin-binding protein from the chicken embryo [l]. A cDNA clone was isolated from a chicken library [2] and the deduced sequence predicts that the retinoic-acid-inducedheparin-binding (RIHB) gene contains 121 amino acids and is very rich in basic amino acids and in cysteine residues. Northern-blot analysis of RNA extracted from whole embryos indicates that the level of RNA expression is high during early embryonic development (day 2), then decreases and is barely detectable by this method after day 15 [2]. The secreted protein is present in basement membranes and around many types of cells, apparently irrespective of their embryonic origins, during early embryogenesis. The RIHB mRNA is expressed in differentiating chondrocytes and the protein is accumulated in the hypertrophic chondrocytes [3], suggesting a role in cartilage differentiation. In vitro, the synthesis of this protein is controlled by retinoic acid in primary cultures of embryonic chicken chondrocytes [4] and myoblasts [5].RIHB belongs to a new heparin-binding protein family of which the principal characteristics are the ability to bind heparin, a molecular mass of approximately 14-15 kDa, basicity, the conservation of cysteine and tryptophan residues in the amino acid sequence, a neurotrophic action and an induction by retinoic acid in some in vitro models. Members of this family include the product of the midgestation kidney (MK) gene characterised in the mouse [6] Abbreviations. RIHB, retinoic-acid-induced heparin-binding; MK, midgestation kidney; HBGAM, heparin-binding growth-associated molecule; RA, retinoic acid.Note. The sequence reported in this paper has deposited with the EMBL data bank and is available under accession number X 76482.(HBGAM), characterised in the rat,mouse, cow, human and in the chicken. This second protein has been assigned several names, reflecting the diverse laboratories in which it was identified (listed in [S]). Sequence similarities and a similar expressi...

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“…Comparison of the RIHB sequence to those in the gene bank revealed that it has considerable homology with two other previously characterized proteins, MK (for mid-gestation kidney) and PTN (pleiotrophin) (reviewed in Bohlen and Kovesdi, 1991). M K was originally cloned as a gene induced by retinoic acid in HM1 teratocarcinoma cells (Kadomatsu et al, 1988), and PTN, known variously as HBNF, HBBM, HB-GAM, HBGF-8, HARP, OSF-1, and p18, has been independently described by many different groups studying diverse tissues (Milner et al, 1989;Rauvala, 1989;Huber et al, 1990;Li et al, 1990;Tezuka et al, 1990;Bohlen and Kovesdi, 1991;Courty et al, 1991). RIHB shares 64% amino acid identity with murine MK, and 50% identity with PTN (regardless of the species).…”

Section: Introductionmentioning

confidence: 99%

Retinoic acid induced heparin‐binding protein expression and localization during gastrulation, neurulation, and organogenesis

Cockshutt

Jonet

Jeanny

et al. 1994

Developmental Dynamics

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Retinoic acid induced heparinbinding protein (RIHB) is a highly basic, soluble polypeptide of the chick embryonic extracellular matrix. We have examined the expression and localization of RIHB during very early embryogenesis by in situ hybridization and immunohistochemistry. RIHB mRNA is very weakly detectable above background in the blastodiscs of unincubated eggs. The expression increases greatly over the first 24 hours of incubation, and is observed throughout the blastodisc in all three of the germ layers following gastrulation. As neurulation occurs, the expression becomes more restricted to certain areas, notably the ectoderm, the neural folds, and especially the notochord. After the neural tube has formed the expression in the tube itself decreases dramatically, whereas the expression in the head ectoderm and the notochord persists. After 72 hours of incubation expression remains relatively high throughout most of the embryo, with higher levels of expression in regions undergoing organogenesis and lower levels in organs which have already differentiated. RIHB protein is also weakly detectable in unincubated eggs as patches of immunoreactive material between the blastodisc and the vitelline. After 6 hours of incubation small regions of basement membrane are immunoreactive. RIHB is detected in this matrix, apparently before even fibronectin. The amount of RIHB protein increases dramatically over the first 24 hours of incubation. It is found in basement membrane separating the epiblast from the hypoblast, then later in that separating the ectoderm from the mesoderm. It is also detected surrounding individual cells, especially of the ectodermal layer. During neurulation RIHB is observed in the basement membrane surrounding the neural fold and the notochord, and in the lamina separating the ectodermal, mesodermal, and endodermal layers. Later in development, RIHB is detected in the basement membrane under the epidermis, throughout the developing limbs, and in the lamina of various developing organs, such as the eye, the pulmonary bud, the intestine, and the mesonephros. These results demonstrate that RIHB is highly expressed during the

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Amino-terminal sequences of a novel heparin-binding protein from human, bovine, rat, and chick brain: High interspecies homology

Cited by 25 publications

References 19 publications

Pig uterine luminal fluid contains the developmentally regulated neurotrophic factor, pleiotrophin

Pig uterine luminal fluid contains the developmentally regulated neurotrophic factor, pleiotrophin

Organisation and Promoter Activity of the Retinoic‐acid‐induced‐heparin‐binding (RIHB) Gene

Retinoic acid induced heparin‐binding protein expression and localization during gastrulation, neurulation, and organogenesis

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