cDNA cloning, sequencing and in situ localization of a transcript specific to both sublingual demilune cells and parotid intercalated duct cells in mouse salivary glands

A cDNA clone derived from mouse sublingual gland was isolated from a λ-phage cDNA library. Northern blot hybridization indicated that the transcript from which it was derived was approx. 700 nucleotides in length. This mRNA encoded a protein of about 20 kDa, as determined by hybrid selection and cel...

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Veröffentlicht in:Archives of oral biology 1994-12, Vol.39 (12), p.1011-1022
Hauptverfasser: Bekhor, Isaac, Wen, Yi, Shi, Songtao, Hsieh, Chih-Hsin, Denny, Patricia A., Denny, Paul C.
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container_end_page 1022
container_issue 12
container_start_page 1011
container_title Archives of oral biology
container_volume 39
creator Bekhor, Isaac
Wen, Yi
Shi, Songtao
Hsieh, Chih-Hsin
Denny, Patricia A.
Denny, Paul C.
description A cDNA clone derived from mouse sublingual gland was isolated from a λ-phage cDNA library. Northern blot hybridization indicated that the transcript from which it was derived was approx. 700 nucleotides in length. This mRNA encoded a protein of about 20 kDa, as determined by hybrid selection and cell-free translation. Conceptual translation of the cDNA clones showed that p20 is 170 amino acids in length. The putative protein is hydrophobic in nature, is neither a mucin-like protein nor does its amino acid sequence or composition resemble the other known mouse proteins. However, the amino acid sequence of p20 suggests that it may be from a gene or gene family homologous to rat common salivary protein 1. The p20 mRNA also appears to share a non-random degree of sequence homology with the cysteine-rich domains of bovine and porcine submandibular mucins. The p20 mRNA is abundant in the mouse sublingual gland, and its expression is approx. nine times greater than in the parotid gland. In situ hybridizations localized the p20 mRNA exclusively in the demilune cells of the sublingual gland and in the intercalated duct cells of the parotid gland. It is detectable in the neonatal and adult submandibular gland at very low levels, but is absent from liver, heart, brain, thymus, spleen, lens and lacrimal glands.
doi_str_mv 10.1016/0003-9969(94)90052-3
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Northern blot hybridization indicated that the transcript from which it was derived was approx. 700 nucleotides in length. This mRNA encoded a protein of about 20 kDa, as determined by hybrid selection and cell-free translation. Conceptual translation of the cDNA clones showed that p20 is 170 amino acids in length. The putative protein is hydrophobic in nature, is neither a mucin-like protein nor does its amino acid sequence or composition resemble the other known mouse proteins. However, the amino acid sequence of p20 suggests that it may be from a gene or gene family homologous to rat common salivary protein 1. The p20 mRNA also appears to share a non-random degree of sequence homology with the cysteine-rich domains of bovine and porcine submandibular mucins. The p20 mRNA is abundant in the mouse sublingual gland, and its expression is approx. nine times greater than in the parotid gland. In situ hybridizations localized the p20 mRNA exclusively in the demilune cells of the sublingual gland and in the intercalated duct cells of the parotid gland. 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Northern blot hybridization indicated that the transcript from which it was derived was approx. 700 nucleotides in length. This mRNA encoded a protein of about 20 kDa, as determined by hybrid selection and cell-free translation. Conceptual translation of the cDNA clones showed that p20 is 170 amino acids in length. The putative protein is hydrophobic in nature, is neither a mucin-like protein nor does its amino acid sequence or composition resemble the other known mouse proteins. However, the amino acid sequence of p20 suggests that it may be from a gene or gene family homologous to rat common salivary protein 1. The p20 mRNA also appears to share a non-random degree of sequence homology with the cysteine-rich domains of bovine and porcine submandibular mucins. The p20 mRNA is abundant in the mouse sublingual gland, and its expression is approx. nine times greater than in the parotid gland. In situ hybridizations localized the p20 mRNA exclusively in the demilune cells of the sublingual gland and in the intercalated duct cells of the parotid gland. 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Wen, Yi ; Shi, Songtao ; Hsieh, Chih-Hsin ; Denny, Patricia A. ; Denny, Paul C.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c357t-5cc5022e65ad64a49f33c3efee93b130aaee6dfc38a3a4b5598ac0776e6d22e43</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1994</creationdate><topic>5′-RACE</topic><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Base Sequence</topic><topic>Blotting, Northern</topic><topic>cDNA cloning</topic><topic>Cloning, Molecular</topic><topic>Dentistry</topic><topic>DNA Primers</topic><topic>DNA Restriction Enzymes</topic><topic>DNA sequencing</topic><topic>DNA, Complementary - isolation &amp; purification</topic><topic>Female</topic><topic>Glycoproteins - biosynthesis</topic><topic>Glycoproteins - chemistry</topic><topic>Glycoproteins - genetics</topic><topic>Immunohistochemistry</topic><topic>In Situ Hybridization</topic><topic>Male</topic><topic>Mice</topic><topic>Molecular Sequence Data</topic><topic>mRNA</topic><topic>Organ Specificity</topic><topic>parotid</topic><topic>Parotid Gland - cytology</topic><topic>Parotid Gland - metabolism</topic><topic>PCR</topic><topic>Polymerase Chain Reaction</topic><topic>Protein Biosynthesis</topic><topic>RNA Probes</topic><topic>RNA, Messenger - analysis</topic><topic>Salivary Proteins and Peptides - biosynthesis</topic><topic>Salivary Proteins and Peptides - chemistry</topic><topic>Salivary Proteins and Peptides - genetics</topic><topic>Sequence Analysis, DNA</topic><topic>Sequence Homology, Amino Acid</topic><topic>Sequence Homology, Nucleic Acid</topic><topic>SLGp20</topic><topic>sublingual</topic><topic>Sublingual Gland - cytology</topic><topic>Sublingual Gland - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Bekhor, Isaac</creatorcontrib><creatorcontrib>Wen, Yi</creatorcontrib><creatorcontrib>Shi, Songtao</creatorcontrib><creatorcontrib>Hsieh, Chih-Hsin</creatorcontrib><creatorcontrib>Denny, Patricia A.</creatorcontrib><creatorcontrib>Denny, Paul C.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Archives of oral biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Bekhor, Isaac</au><au>Wen, Yi</au><au>Shi, Songtao</au><au>Hsieh, Chih-Hsin</au><au>Denny, Patricia A.</au><au>Denny, Paul C.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>cDNA cloning, sequencing and in situ localization of a transcript specific to both sublingual demilune cells and parotid intercalated duct cells in mouse salivary glands</atitle><jtitle>Archives of oral biology</jtitle><addtitle>Arch Oral Biol</addtitle><date>1994-12-01</date><risdate>1994</risdate><volume>39</volume><issue>12</issue><spage>1011</spage><epage>1022</epage><pages>1011-1022</pages><issn>0003-9969</issn><eissn>1879-1506</eissn><abstract>A cDNA clone derived from mouse sublingual gland was isolated from a λ-phage cDNA library. Northern blot hybridization indicated that the transcript from which it was derived was approx. 700 nucleotides in length. This mRNA encoded a protein of about 20 kDa, as determined by hybrid selection and cell-free translation. Conceptual translation of the cDNA clones showed that p20 is 170 amino acids in length. The putative protein is hydrophobic in nature, is neither a mucin-like protein nor does its amino acid sequence or composition resemble the other known mouse proteins. However, the amino acid sequence of p20 suggests that it may be from a gene or gene family homologous to rat common salivary protein 1. The p20 mRNA also appears to share a non-random degree of sequence homology with the cysteine-rich domains of bovine and porcine submandibular mucins. The p20 mRNA is abundant in the mouse sublingual gland, and its expression is approx. nine times greater than in the parotid gland. In situ hybridizations localized the p20 mRNA exclusively in the demilune cells of the sublingual gland and in the intercalated duct cells of the parotid gland. It is detectable in the neonatal and adult submandibular gland at very low levels, but is absent from liver, heart, brain, thymus, spleen, lens and lacrimal glands.</abstract><cop>England</cop><pub>Elsevier Ltd</pub><pmid>7717881</pmid><doi>10.1016/0003-9969(94)90052-3</doi><tpages>12</tpages></addata></record>
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ispartof Archives of oral biology, 1994-12, Vol.39 (12), p.1011-1022
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source MEDLINE; ScienceDirect Journals (5 years ago - present)
subjects 5′-RACE
Amino Acid Sequence
Animals
Base Sequence
Blotting, Northern
cDNA cloning
Cloning, Molecular
Dentistry
DNA Primers
DNA Restriction Enzymes
DNA sequencing
DNA, Complementary - isolation & purification
Female
Glycoproteins - biosynthesis
Glycoproteins - chemistry
Glycoproteins - genetics
Immunohistochemistry
In Situ Hybridization
Male
Mice
Molecular Sequence Data
mRNA
Organ Specificity
parotid
Parotid Gland - cytology
Parotid Gland - metabolism
PCR
Polymerase Chain Reaction
Protein Biosynthesis
RNA Probes
RNA, Messenger - analysis
Salivary Proteins and Peptides - biosynthesis
Salivary Proteins and Peptides - chemistry
Salivary Proteins and Peptides - genetics
Sequence Analysis, DNA
Sequence Homology, Amino Acid
Sequence Homology, Nucleic Acid
SLGp20
sublingual
Sublingual Gland - cytology
Sublingual Gland - metabolism
title cDNA cloning, sequencing and in situ localization of a transcript specific to both sublingual demilune cells and parotid intercalated duct cells in mouse salivary glands
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