Expression of spasmolysin (FIM-A.1): an integumentary mucin from Xenopus laevis
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Expression of spasmolysin (FIM-A.1) : an integumentary mucin from Xenopus laevis. / Hauser, F; Gertzen, E M; Hoffmann, W.
In: Experimental Cell Research, Vol. 189, No. 2, 08.1990, p. 157-62.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - Expression of spasmolysin (FIM-A.1)
T2 - an integumentary mucin from Xenopus laevis
AU - Hauser, F
AU - Gertzen, E M
AU - Hoffmann, W
PY - 1990/8
Y1 - 1990/8
N2 - In the past, a unique type of precursor for a secretory protein was discovered. It contains a central repetitive domain rich in threonine residues and terminal cysteine-rich domains. Due to striking homologies of these terminal domains with pancreatic spasmolytic polypeptide, originally the name "prepro-spasmolysin" was proposed. Here we show that the mature protein has a MW of about 130 kDa, consisting of about 70% carbohydrate and 30% protein. Similar O-linked glycoproteins have been found in mucins from human intestine. For this and numerous other reasons we decided to rename this glycoprotein "frog integumentary mucin A.1" (FIM-A.1). Furthermore, analysis of the protein with specific antibodies against the predicted C-terminal end indicates that FIM-A.1 is probably not processed at pairs of basic residues. In situ hybridization as well as immunofluorescence studies revealed that FIM-A.1 is expressed and stored exclusively in mature mucous glands of Xenopus laevis skin. Only cone cells at the proximal part of these glands do not synthesize FIM-A.1. In contrast, all other physiologically active peptides from X. laevis skin investigated so far are synthesized in granular glands. A hypothetical function of FIMs for defense against microbial infections is discussed.
AB - In the past, a unique type of precursor for a secretory protein was discovered. It contains a central repetitive domain rich in threonine residues and terminal cysteine-rich domains. Due to striking homologies of these terminal domains with pancreatic spasmolytic polypeptide, originally the name "prepro-spasmolysin" was proposed. Here we show that the mature protein has a MW of about 130 kDa, consisting of about 70% carbohydrate and 30% protein. Similar O-linked glycoproteins have been found in mucins from human intestine. For this and numerous other reasons we decided to rename this glycoprotein "frog integumentary mucin A.1" (FIM-A.1). Furthermore, analysis of the protein with specific antibodies against the predicted C-terminal end indicates that FIM-A.1 is probably not processed at pairs of basic residues. In situ hybridization as well as immunofluorescence studies revealed that FIM-A.1 is expressed and stored exclusively in mature mucous glands of Xenopus laevis skin. Only cone cells at the proximal part of these glands do not synthesize FIM-A.1. In contrast, all other physiologically active peptides from X. laevis skin investigated so far are synthesized in granular glands. A hypothetical function of FIMs for defense against microbial infections is discussed.
KW - Amino Acid Sequence
KW - Animals
KW - Base Sequence
KW - Electrophoresis, Polyacrylamide Gel
KW - Fluorescent Antibody Technique
KW - Immune Sera
KW - Molecular Sequence Data
KW - Molecular Weight
KW - Mucins/analysis
KW - Mucous Membrane/cytology
KW - Oligonucleotide Probes
KW - Oligopeptides/chemical synthesis
KW - Recombinant Fusion Proteins/analysis
KW - Skin/cytology
KW - Xenopus Proteins
KW - Xenopus laevis
U2 - 10.1016/0014-4827(90)90230-8
DO - 10.1016/0014-4827(90)90230-8
M3 - Journal article
C2 - 2196180
VL - 189
SP - 157
EP - 162
JO - Experimental Cell Research
JF - Experimental Cell Research
SN - 0014-4827
IS - 2
ER -
ID: 347886198