The polymorphic integumentary mucin B.1 from Xenopus laevis contains the short consensus repeat
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The polymorphic integumentary mucin B.1 from Xenopus laevis contains the short consensus repeat. / Probst, J C; Hauser, F; Joba, W; Hoffmann, W.
In: The Journal of Biological Chemistry, Vol. 267, No. 9, 25.03.1992, p. 6310-6.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - The polymorphic integumentary mucin B.1 from Xenopus laevis contains the short consensus repeat
AU - Probst, J C
AU - Hauser, F
AU - Joba, W
AU - Hoffmann, W
PY - 1992/3/25
Y1 - 1992/3/25
N2 - The frog integumentary mucin B.1 (FIM-B.1), discovered by molecular cloning, contains a cysteine-rich C-terminal domain which is homologous with von Willebrand factor. With the help of the polymerase chain reaction, we now characterize a contiguous region 5' to the von Willebrand factor domain containing the short consensus repeat typical of many proteins from the complement system. Multiple transcripts have been cloned, which originate from a single animal and differ by a variable number of tandem repeats (rep-33 sequences). These different transcripts probably originate solely from two genes and are generated presumably by alternative splicing of an huge array of functional cassettes. This model is supported by analysis of genomic FIM-B.1 sequences from Xenopus laevis. Here, rep-33 sequences are arranged in an interrupted array of individual units. Additionally, results of Southern analysis revealed genetic polymorphism between different animals which is predicted to be within the tandem repeats. A first investigation of the predicted mucins with the help of a specific antibody against a synthetic peptide determined the molecular mass of FIM-B.1 to greater than 200 kDa. Here again, genetic polymorphism between different animals is detected.
AB - The frog integumentary mucin B.1 (FIM-B.1), discovered by molecular cloning, contains a cysteine-rich C-terminal domain which is homologous with von Willebrand factor. With the help of the polymerase chain reaction, we now characterize a contiguous region 5' to the von Willebrand factor domain containing the short consensus repeat typical of many proteins from the complement system. Multiple transcripts have been cloned, which originate from a single animal and differ by a variable number of tandem repeats (rep-33 sequences). These different transcripts probably originate solely from two genes and are generated presumably by alternative splicing of an huge array of functional cassettes. This model is supported by analysis of genomic FIM-B.1 sequences from Xenopus laevis. Here, rep-33 sequences are arranged in an interrupted array of individual units. Additionally, results of Southern analysis revealed genetic polymorphism between different animals which is predicted to be within the tandem repeats. A first investigation of the predicted mucins with the help of a specific antibody against a synthetic peptide determined the molecular mass of FIM-B.1 to greater than 200 kDa. Here again, genetic polymorphism between different animals is detected.
KW - Amino Acid Sequence
KW - Animals
KW - Base Sequence
KW - Cloning, Molecular
KW - DNA/genetics
KW - Humans
KW - Liver/physiology
KW - Molecular Sequence Data
KW - Mucins/genetics
KW - Oligodeoxyribonucleotides
KW - Polymerase Chain Reaction
KW - Polymorphism, Genetic
KW - RNA, Messenger/genetics
KW - Repetitive Sequences, Nucleic Acid
KW - Restriction Mapping
KW - Sequence Homology, Nucleic Acid
KW - Skin Physiological Phenomena
KW - Xenopus Proteins
KW - Xenopus laevis
M3 - Journal article
C2 - 1556137
VL - 267
SP - 6310
EP - 6316
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 9
ER -
ID: 347886112