xP2, a new member of the P-domain peptide family of potential growth factors, is synthesized in Xenopus laevis skin

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

xP2, a new member of the P-domain peptide family of potential growth factors, is synthesized in Xenopus laevis skin. / Hauser, F; Roeben, C; Hoffmann, W.

In: The Journal of Biological Chemistry, Vol. 267, No. 20, 15.07.1992, p. 14451-5.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Hauser, F, Roeben, C & Hoffmann, W 1992, 'xP2, a new member of the P-domain peptide family of potential growth factors, is synthesized in Xenopus laevis skin', The Journal of Biological Chemistry, vol. 267, no. 20, pp. 14451-5.

APA

Hauser, F., Roeben, C., & Hoffmann, W. (1992). xP2, a new member of the P-domain peptide family of potential growth factors, is synthesized in Xenopus laevis skin. The Journal of Biological Chemistry, 267(20), 14451-5.

Vancouver

Hauser F, Roeben C, Hoffmann W. xP2, a new member of the P-domain peptide family of potential growth factors, is synthesized in Xenopus laevis skin. The Journal of Biological Chemistry. 1992 Jul 15;267(20):14451-5.

Author

Hauser, F ; Roeben, C ; Hoffmann, W. / xP2, a new member of the P-domain peptide family of potential growth factors, is synthesized in Xenopus laevis skin. In: The Journal of Biological Chemistry. 1992 ; Vol. 267, No. 20. pp. 14451-5.

Bibtex

@article{ed356d91874645e490dcb0c751d2f80c,
title = "xP2, a new member of the P-domain peptide family of potential growth factors, is synthesized in Xenopus laevis skin",
abstract = "Similarly to epidermal growth factor (EGF) and EGF-like repeats, the {"}P-domain{"} represents a cysteine-rich module that has been detected in the past in a variety of polypeptides, as well as in high molecular weight proteins. Here, a precursor for a secretory polypeptide (xP2) is characterized that consists of two P-domains. xP2 has been discovered in Xenopus laevis with the help of the polymerase chain reaction. In contrast to all other P-domain peptides, it is synthesized in the skin but not in the stomach or the pancreas. By this and other criteria, it cannot be considered simply as the X. laevis homologue of recently described P-domain peptides, viz. the spasmolytic polypeptides (PSP/hSP/mSP). Furthermore, a polyclonal antiserum was generated against the deduced C-terminal end of xP2. Due to its immunoreactivity with granular glands, as well as with the epidermis, the possibility of a growth factor activity for xP2 in the germinal layer is discussed.",
keywords = "Amino Acid Sequence, Animals, Antibodies, Blotting, Western, Cloning, Molecular, DNA/genetics, Electrophoresis, Polyacrylamide Gel, Growth Substances/analysis, Immunohistochemistry, Molecular Sequence Data, Molecular Weight, Oligodeoxyribonucleotides, Peptides/chemical synthesis, Polymerase Chain Reaction/methods, RNA, Messenger/genetics, Sequence Homology, Nucleic Acid, Skin/metabolism, Templates, Genetic, Xenopus Proteins, Xenopus laevis",
author = "F Hauser and C Roeben and W Hoffmann",
year = "1992",
month = jul,
day = "15",
language = "English",
volume = "267",
pages = "14451--5",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology, Inc.",
number = "20",

}

RIS

TY - JOUR

T1 - xP2, a new member of the P-domain peptide family of potential growth factors, is synthesized in Xenopus laevis skin

AU - Hauser, F

AU - Roeben, C

AU - Hoffmann, W

PY - 1992/7/15

Y1 - 1992/7/15

N2 - Similarly to epidermal growth factor (EGF) and EGF-like repeats, the "P-domain" represents a cysteine-rich module that has been detected in the past in a variety of polypeptides, as well as in high molecular weight proteins. Here, a precursor for a secretory polypeptide (xP2) is characterized that consists of two P-domains. xP2 has been discovered in Xenopus laevis with the help of the polymerase chain reaction. In contrast to all other P-domain peptides, it is synthesized in the skin but not in the stomach or the pancreas. By this and other criteria, it cannot be considered simply as the X. laevis homologue of recently described P-domain peptides, viz. the spasmolytic polypeptides (PSP/hSP/mSP). Furthermore, a polyclonal antiserum was generated against the deduced C-terminal end of xP2. Due to its immunoreactivity with granular glands, as well as with the epidermis, the possibility of a growth factor activity for xP2 in the germinal layer is discussed.

AB - Similarly to epidermal growth factor (EGF) and EGF-like repeats, the "P-domain" represents a cysteine-rich module that has been detected in the past in a variety of polypeptides, as well as in high molecular weight proteins. Here, a precursor for a secretory polypeptide (xP2) is characterized that consists of two P-domains. xP2 has been discovered in Xenopus laevis with the help of the polymerase chain reaction. In contrast to all other P-domain peptides, it is synthesized in the skin but not in the stomach or the pancreas. By this and other criteria, it cannot be considered simply as the X. laevis homologue of recently described P-domain peptides, viz. the spasmolytic polypeptides (PSP/hSP/mSP). Furthermore, a polyclonal antiserum was generated against the deduced C-terminal end of xP2. Due to its immunoreactivity with granular glands, as well as with the epidermis, the possibility of a growth factor activity for xP2 in the germinal layer is discussed.

KW - Amino Acid Sequence

KW - Animals

KW - Antibodies

KW - Blotting, Western

KW - Cloning, Molecular

KW - DNA/genetics

KW - Electrophoresis, Polyacrylamide Gel

KW - Growth Substances/analysis

KW - Immunohistochemistry

KW - Molecular Sequence Data

KW - Molecular Weight

KW - Oligodeoxyribonucleotides

KW - Peptides/chemical synthesis

KW - Polymerase Chain Reaction/methods

KW - RNA, Messenger/genetics

KW - Sequence Homology, Nucleic Acid

KW - Skin/metabolism

KW - Templates, Genetic

KW - Xenopus Proteins

KW - Xenopus laevis

M3 - Journal article

C2 - 1629230

VL - 267

SP - 14451

EP - 14455

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 20

ER -

ID: 347886074