Molecular cloning and expression of collagenase-3, a novel human matrix metalloproteinase produced by breast carcinomas
A cDNA coding for a new human matrix metalloproteinase (MMP) has been cloned from a cDNA library derived from a breast tumor. The isolated cDNA contains an open reading frame coding for a polypeptide of 471 amino acids. The predicted protein sequence displays extensive similarity to the previously k...
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| Veröffentlicht in: | The Journal of biological chemistry 1994-06, Vol.269 (24), p.16766-16773 |
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| creator | Freije, J M Díez-Itza, I Balbín, M Sánchez, L M Blasco, R Tolivia, J López-Otín, C |
| description | A cDNA coding for a new human matrix metalloproteinase (MMP) has been cloned from a cDNA library derived from a breast tumor.
The isolated cDNA contains an open reading frame coding for a polypeptide of 471 amino acids. The predicted protein sequence
displays extensive similarity to the previously known MMPs and presents all the structural features characteristic of the
members of this protein family, including the well conserved PRCGXPD motif, involved in the latency of the enzyme and the
zinc-binding domain (HEXGHXXXXXHS). In addition, this novel human MMP contains in its amino acid sequence several residues
specific to the collagenase subfamily (Tyr-214, Asp-235, and Gly-237) and lacks the 9-residue insertion present in the stromelysins.
According to these structural characteristics, the MMP described herein has been tentatively called collagenase-3, since it
represents the third member of this subfamily, composed at present of fibroblast and neutrophil collagenases. The collagenase-3
cDNA was expressed in a vaccinia virus system, and the recombinant protein was able to degrade fibrillar collagens, providing
support to the hypothesis that the isolated cDNA codes for an authentic collagenase. Northern blot analysis of RNA from normal
and pathological tissues demonstrated the existence in breast tumors of three different mRNA species, which seem to be the
result of the utilization of different polyadenylation sites present in the 3'-noncoding region of the gene. By contrast,
no collagenase-3 mRNA was detected either by Northern blot or RNA polymerase chain reaction analysis with RNA from other human
tissues, including normal breast, mammary fibroadenomas, liver, placenta, ovary, uterus, prostate, and parotid gland. On the
basis of the increased expression of collagenase-3 in breast carcinomas and the absence of detectable expression in normal
tissues, a possible role for this metalloproteinase in the tumoral process is proposed. |
| doi_str_mv | 10.1016/s0021-9258(19)89457-7 |
| format | Article |
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The isolated cDNA contains an open reading frame coding for a polypeptide of 471 amino acids. The predicted protein sequence
displays extensive similarity to the previously known MMPs and presents all the structural features characteristic of the
members of this protein family, including the well conserved PRCGXPD motif, involved in the latency of the enzyme and the
zinc-binding domain (HEXGHXXXXXHS). In addition, this novel human MMP contains in its amino acid sequence several residues
specific to the collagenase subfamily (Tyr-214, Asp-235, and Gly-237) and lacks the 9-residue insertion present in the stromelysins.
According to these structural characteristics, the MMP described herein has been tentatively called collagenase-3, since it
represents the third member of this subfamily, composed at present of fibroblast and neutrophil collagenases. The collagenase-3
cDNA was expressed in a vaccinia virus system, and the recombinant protein was able to degrade fibrillar collagens, providing
support to the hypothesis that the isolated cDNA codes for an authentic collagenase. Northern blot analysis of RNA from normal
and pathological tissues demonstrated the existence in breast tumors of three different mRNA species, which seem to be the
result of the utilization of different polyadenylation sites present in the 3'-noncoding region of the gene. By contrast,
no collagenase-3 mRNA was detected either by Northern blot or RNA polymerase chain reaction analysis with RNA from other human
tissues, including normal breast, mammary fibroadenomas, liver, placenta, ovary, uterus, prostate, and parotid gland. On the
basis of the increased expression of collagenase-3 in breast carcinomas and the absence of detectable expression in normal
tissues, a possible role for this metalloproteinase in the tumoral process is proposed.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/s0021-9258(19)89457-7</identifier><identifier>PMID: 8207000</identifier><identifier>CODEN: JBCHA3</identifier><language>eng</language><publisher>Bethesda, MD: American Society for Biochemistry and Molecular Biology</publisher><subject>Amino Acid Sequence ; Analytical, structural and metabolic biochemistry ; Base Sequence ; Biological and medical sciences ; breast ; Breast Neoplasms - enzymology ; Breast Neoplasms - pathology ; carcinoma ; cDNA ; Cloning, Molecular ; collagenase 3 ; Collagenases - biosynthesis ; Collagenases - chemistry ; Collagenases - genetics ; Conserved Sequence ; Enzymes and enzyme inhibitors ; Escherichia coli ; Female ; Fundamental and applied biological sciences. Psychology ; Gene Expression ; Gene Library ; genes ; Humans ; Hydrolases ; Immunohistochemistry ; man ; Matrix Metalloproteinase 13 ; Matrix Metalloproteinase 3 ; Metalloendopeptidases - chemistry ; Metalloendopeptidases - genetics ; Molecular Sequence Data ; nucleotide sequence ; Oligodeoxyribonucleotides ; Polymerase Chain Reaction - methods ; prediction ; RNA, Neoplasm - isolation & purification ; RNA, Neoplasm - metabolism ; Sequence Homology, Amino Acid</subject><ispartof>The Journal of biological chemistry, 1994-06, Vol.269 (24), p.16766-16773</ispartof><rights>1994 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c558t-e9434e21123844303aa481531b0d8dcb00ba6603987826ad6dcc1e7c2566b9053</citedby><cites>FETCH-LOGICAL-c558t-e9434e21123844303aa481531b0d8dcb00ba6603987826ad6dcc1e7c2566b9053</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27903,27904</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=4216124$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8207000$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Freije, J M</creatorcontrib><creatorcontrib>Díez-Itza, I</creatorcontrib><creatorcontrib>Balbín, M</creatorcontrib><creatorcontrib>Sánchez, L M</creatorcontrib><creatorcontrib>Blasco, R</creatorcontrib><creatorcontrib>Tolivia, J</creatorcontrib><creatorcontrib>López-Otín, C</creatorcontrib><title>Molecular cloning and expression of collagenase-3, a novel human matrix metalloproteinase produced by breast carcinomas</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>A cDNA coding for a new human matrix metalloproteinase (MMP) has been cloned from a cDNA library derived from a breast tumor.
The isolated cDNA contains an open reading frame coding for a polypeptide of 471 amino acids. The predicted protein sequence
displays extensive similarity to the previously known MMPs and presents all the structural features characteristic of the
members of this protein family, including the well conserved PRCGXPD motif, involved in the latency of the enzyme and the
zinc-binding domain (HEXGHXXXXXHS). In addition, this novel human MMP contains in its amino acid sequence several residues
specific to the collagenase subfamily (Tyr-214, Asp-235, and Gly-237) and lacks the 9-residue insertion present in the stromelysins.
According to these structural characteristics, the MMP described herein has been tentatively called collagenase-3, since it
represents the third member of this subfamily, composed at present of fibroblast and neutrophil collagenases. The collagenase-3
cDNA was expressed in a vaccinia virus system, and the recombinant protein was able to degrade fibrillar collagens, providing
support to the hypothesis that the isolated cDNA codes for an authentic collagenase. Northern blot analysis of RNA from normal
and pathological tissues demonstrated the existence in breast tumors of three different mRNA species, which seem to be the
result of the utilization of different polyadenylation sites present in the 3'-noncoding region of the gene. By contrast,
no collagenase-3 mRNA was detected either by Northern blot or RNA polymerase chain reaction analysis with RNA from other human
tissues, including normal breast, mammary fibroadenomas, liver, placenta, ovary, uterus, prostate, and parotid gland. On the
basis of the increased expression of collagenase-3 in breast carcinomas and the absence of detectable expression in normal
tissues, a possible role for this metalloproteinase in the tumoral process is proposed.</description><subject>Amino Acid Sequence</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Base Sequence</subject><subject>Biological and medical sciences</subject><subject>breast</subject><subject>Breast Neoplasms - enzymology</subject><subject>Breast Neoplasms - pathology</subject><subject>carcinoma</subject><subject>cDNA</subject><subject>Cloning, Molecular</subject><subject>collagenase 3</subject><subject>Collagenases - biosynthesis</subject><subject>Collagenases - chemistry</subject><subject>Collagenases - genetics</subject><subject>Conserved Sequence</subject><subject>Enzymes and enzyme inhibitors</subject><subject>Escherichia coli</subject><subject>Female</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gene Expression</subject><subject>Gene Library</subject><subject>genes</subject><subject>Humans</subject><subject>Hydrolases</subject><subject>Immunohistochemistry</subject><subject>man</subject><subject>Matrix Metalloproteinase 13</subject><subject>Matrix Metalloproteinase 3</subject><subject>Metalloendopeptidases - chemistry</subject><subject>Metalloendopeptidases - genetics</subject><subject>Molecular Sequence Data</subject><subject>nucleotide sequence</subject><subject>Oligodeoxyribonucleotides</subject><subject>Polymerase Chain Reaction - methods</subject><subject>prediction</subject><subject>RNA, Neoplasm - isolation & purification</subject><subject>RNA, Neoplasm - metabolism</subject><subject>Sequence Homology, Amino Acid</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1994</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkU1vEzEQhi1EVULhJ1TyASGQWPD32seq4ktqxQGQuFle7yQx8trB3qXtv8ehUXqsL2NrnhnPvC9C55S8p4SqD5UQRjvDpH5DzVtthOy7_glaUaJ5xyX99RStjsgz9LzW36QdYegpOtWM9O2xQjfXOYJfoivYx5xC2mCXRgy3uwK1hpxwXmOfY3QbSK5Cx99hh1P-CxFvl8klPLm5hFs8wexizLuSZwh7ErfruHgY8XCHhwKuzti74kPKk6sv0MnaxQovD_EM_fz08cfll-7q2-evlxdXnZdSzx0YwQUwShnXQnDCnROaSk4HMurRD4QMTinCje41U25Uo_cUes-kUoMhkp-h1_d92zR_FqiznUL10PZJkJdqeyW5IlI8ClJlVJOTNFDeg77kWgus7a6EyZU7S4ndO2O_72W3e9ktNfa_M7ZvdeeHD5ZhgvFYdbCi5V8d8q56F9fFJR_qEROMKsrEA7YNm-1NKGCHkP0WJsuUsUy0QXul-D8zvqKl</recordid><startdate>19940617</startdate><enddate>19940617</enddate><creator>Freije, J M</creator><creator>Díez-Itza, I</creator><creator>Balbín, M</creator><creator>Sánchez, L M</creator><creator>Blasco, R</creator><creator>Tolivia, J</creator><creator>López-Otín, C</creator><general>American Society for Biochemistry and Molecular Biology</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7T3</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>19940617</creationdate><title>Molecular cloning and expression of collagenase-3, a novel human matrix metalloproteinase produced by breast carcinomas</title><author>Freije, J M ; Díez-Itza, I ; Balbín, M ; Sánchez, L M ; Blasco, R ; Tolivia, J ; López-Otín, C</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c558t-e9434e21123844303aa481531b0d8dcb00ba6603987826ad6dcc1e7c2566b9053</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1994</creationdate><topic>Amino Acid Sequence</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Base Sequence</topic><topic>Biological and medical sciences</topic><topic>breast</topic><topic>Breast Neoplasms - enzymology</topic><topic>Breast Neoplasms - pathology</topic><topic>carcinoma</topic><topic>cDNA</topic><topic>Cloning, Molecular</topic><topic>collagenase 3</topic><topic>Collagenases - biosynthesis</topic><topic>Collagenases - chemistry</topic><topic>Collagenases - genetics</topic><topic>Conserved Sequence</topic><topic>Enzymes and enzyme inhibitors</topic><topic>Escherichia coli</topic><topic>Female</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gene Expression</topic><topic>Gene Library</topic><topic>genes</topic><topic>Humans</topic><topic>Hydrolases</topic><topic>Immunohistochemistry</topic><topic>man</topic><topic>Matrix Metalloproteinase 13</topic><topic>Matrix Metalloproteinase 3</topic><topic>Metalloendopeptidases - chemistry</topic><topic>Metalloendopeptidases - genetics</topic><topic>Molecular Sequence Data</topic><topic>nucleotide sequence</topic><topic>Oligodeoxyribonucleotides</topic><topic>Polymerase Chain Reaction - methods</topic><topic>prediction</topic><topic>RNA, Neoplasm - isolation & purification</topic><topic>RNA, Neoplasm - metabolism</topic><topic>Sequence Homology, Amino Acid</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Freije, J M</creatorcontrib><creatorcontrib>Díez-Itza, I</creatorcontrib><creatorcontrib>Balbín, M</creatorcontrib><creatorcontrib>Sánchez, L M</creatorcontrib><creatorcontrib>Blasco, R</creatorcontrib><creatorcontrib>Tolivia, J</creatorcontrib><creatorcontrib>López-Otín, C</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Human Genome Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Freije, J M</au><au>Díez-Itza, I</au><au>Balbín, M</au><au>Sánchez, L M</au><au>Blasco, R</au><au>Tolivia, J</au><au>López-Otín, C</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Molecular cloning and expression of collagenase-3, a novel human matrix metalloproteinase produced by breast carcinomas</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1994-06-17</date><risdate>1994</risdate><volume>269</volume><issue>24</issue><spage>16766</spage><epage>16773</epage><pages>16766-16773</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><coden>JBCHA3</coden><abstract>A cDNA coding for a new human matrix metalloproteinase (MMP) has been cloned from a cDNA library derived from a breast tumor.
The isolated cDNA contains an open reading frame coding for a polypeptide of 471 amino acids. The predicted protein sequence
displays extensive similarity to the previously known MMPs and presents all the structural features characteristic of the
members of this protein family, including the well conserved PRCGXPD motif, involved in the latency of the enzyme and the
zinc-binding domain (HEXGHXXXXXHS). In addition, this novel human MMP contains in its amino acid sequence several residues
specific to the collagenase subfamily (Tyr-214, Asp-235, and Gly-237) and lacks the 9-residue insertion present in the stromelysins.
According to these structural characteristics, the MMP described herein has been tentatively called collagenase-3, since it
represents the third member of this subfamily, composed at present of fibroblast and neutrophil collagenases. The collagenase-3
cDNA was expressed in a vaccinia virus system, and the recombinant protein was able to degrade fibrillar collagens, providing
support to the hypothesis that the isolated cDNA codes for an authentic collagenase. Northern blot analysis of RNA from normal
and pathological tissues demonstrated the existence in breast tumors of three different mRNA species, which seem to be the
result of the utilization of different polyadenylation sites present in the 3'-noncoding region of the gene. By contrast,
no collagenase-3 mRNA was detected either by Northern blot or RNA polymerase chain reaction analysis with RNA from other human
tissues, including normal breast, mammary fibroadenomas, liver, placenta, ovary, uterus, prostate, and parotid gland. On the
basis of the increased expression of collagenase-3 in breast carcinomas and the absence of detectable expression in normal
tissues, a possible role for this metalloproteinase in the tumoral process is proposed.</abstract><cop>Bethesda, MD</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>8207000</pmid><doi>10.1016/s0021-9258(19)89457-7</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | The Journal of biological chemistry, 1994-06, Vol.269 (24), p.16766-16773 |
| issn | 0021-9258 1083-351X |
| language | eng |
| recordid | cdi_proquest_miscellaneous_76536054 |
| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | Amino Acid Sequence Analytical, structural and metabolic biochemistry Base Sequence Biological and medical sciences breast Breast Neoplasms - enzymology Breast Neoplasms - pathology carcinoma cDNA Cloning, Molecular collagenase 3 Collagenases - biosynthesis Collagenases - chemistry Collagenases - genetics Conserved Sequence Enzymes and enzyme inhibitors Escherichia coli Female Fundamental and applied biological sciences. Psychology Gene Expression Gene Library genes Humans Hydrolases Immunohistochemistry man Matrix Metalloproteinase 13 Matrix Metalloproteinase 3 Metalloendopeptidases - chemistry Metalloendopeptidases - genetics Molecular Sequence Data nucleotide sequence Oligodeoxyribonucleotides Polymerase Chain Reaction - methods prediction RNA, Neoplasm - isolation & purification RNA, Neoplasm - metabolism Sequence Homology, Amino Acid |
| title | Molecular cloning and expression of collagenase-3, a novel human matrix metalloproteinase produced by breast carcinomas |
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