Involvement of matrix metalloproteinase‐2 activity in invasion and metastasis of pancreatic carcinoma
BACKGROUND Activation of matrix metalloproteinase‐2 (MMP‐2) has been implicated in the progression, invasion, and metastasis of various cancers, but little information is available with regard to its role in pancreatic carcinoma with poor prognosis. METHODS Gelatin zymography was used for the detect...
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| Veröffentlicht in: | Cancer 1998-02, Vol.82 (4), p.642-650 |
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| creator | Koshiba, Takatomo Hosotani, Ryo Wada, Michihiko Miyamoto, Yoshiharu Fujimoto, Koji Lee, Jeon‐Uk Doi, Ryuichiro Arii, Shigeki Imamura, Masayuki |
| description | BACKGROUND
Activation of matrix metalloproteinase‐2 (MMP‐2) has been implicated in the progression, invasion, and metastasis of various cancers, but little information is available with regard to its role in pancreatic carcinoma with poor prognosis.
METHODS
Gelatin zymography was used for the detection of latent and activated forms of MMP‐2 and MMP‐9 in 13 normal pancreatic tissue specimens, 14 chronic pancreatitis tissue specimens, and 33 pancreatic carcinoma tissue specimens. The gelatinase activity was quantified by densitometer, and the 66‐kilodalton (kDa)/(66‐kDa + 72‐kDa) ratio was calculated as the MMP‐2 activation ratio. Western blot analysis was performed to confirm the zymographic profile.
RESULTS
Latent forms of MMP‐2 and MMP‐9 were detected in all samples of pancreatic carcinoma, chronic pancreatitis, and normal pancreatic tissue. The expression rate of the MMP‐2 activated form in pancreatic carcinoma tissue specimens was 100% (33 of 33) but that of MMP‐9 was 21%. The MMP‐2 activation ratio in pancreatic carcinoma tissue specimens was significantly higher than that of chronic pancreatitis and normal pancreatic tissue specimens. The MMP‐2 activation ratio in pT3 tumors was significantly higher than that in pT1 tumors. The MMP‐2 activation ratio also was significantly higher in pancreatic carcinoma specimens with histologically positive regional lymph node metastasis and distant metastasis than those without metastasis. The MMP‐2 activation ratio observed in patients who developed postresection recurrence within 6 months was significantly higher than that in patients without recurrence at 6 months.
CONCLUSIONS
The results of the current study indicate that MMP‐2 activation plays a significant role in tumor invasion and metastasis in pancreatic carcinoma. Cancer 1998;82:642‐50. © 1998 American Cancer Society.
In this study, the activated form of matrix metalloproteinase‐2 (MMP‐2) was detected in pancreatic carcinoma, chronic pancreatitis, and normal pancreatic tissue specimens by zymographic analysis. The activation of MMP‐2 plays an important role in tumor invasion and metastasis in pancreatic carcinoma. |
| doi_str_mv | 10.1002/(SICI)1097-0142(19980215)82:4<642::AID-CNCR5>3.0.CO;2-N |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_79694594</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>79694594</sourcerecordid><originalsourceid>FETCH-LOGICAL-c4755-180007e26aa79ac5aba38da5443e67708c22daef69e02b809ae7a7a0174498d13</originalsourceid><addsrcrecordid>eNqFkd1q2zAYhsXY6NJulzDwwRjtgTNJliwrGy3F-zOUBPbDevbxRZaHhn9Sy8mWs11Cr7FXMrnJcrLBQCCk79Wrh_cl5ILRKaOUvzz9VOTFGaNaxZQJfsq0zihn8izjM_E6FXw2uyzexPk8_yjPkymd5otXPJ4_IJPDm4dkQinNYimS68fk2Pvv4ai4TI7IkRZKUS0n5FvRbrp6YxvbDlFXRQ0OvfsZNXbAuu5WfTdY16K3d79ueYRmcBs3bCPXhrVB77o2wra8l_uwnB89Vtia3uLgTGSwN67tGnxCHlVYe_t0v5-QL-_efs4_xFeL90V-eRUboaSMWTYyWp4iKo1G4hKTrEQpRGLTgJwZzku0Vaot5cuMarQKFVKmhNBZyZIT8mLnG9Bv1tYP0DhvbF1ja7u1B6VTLaQWQfh1JzR9531vK1j1rsF-C4zCWAHAWAGMccIYJ_ypADIOAkIFAKECuK8AEqCQL4DDPDg_2yOsl40tD777zMP8-X6O3mBd9SEu5w-y8IPQyQh4vZP9cLXd_kX3X7h_se0ukt-41LFY</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>79694594</pqid></control><display><type>article</type><title>Involvement of matrix metalloproteinase‐2 activity in invasion and metastasis of pancreatic carcinoma</title><source>Wiley Free Content</source><source>MEDLINE</source><source>Wiley Online Library Journals Frontfile Complete</source><source>Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals</source><source>Alma/SFX Local Collection</source><creator>Koshiba, Takatomo ; Hosotani, Ryo ; Wada, Michihiko ; Miyamoto, Yoshiharu ; Fujimoto, Koji ; Lee, Jeon‐Uk ; Doi, Ryuichiro ; Arii, Shigeki ; Imamura, Masayuki</creator><creatorcontrib>Koshiba, Takatomo ; Hosotani, Ryo ; Wada, Michihiko ; Miyamoto, Yoshiharu ; Fujimoto, Koji ; Lee, Jeon‐Uk ; Doi, Ryuichiro ; Arii, Shigeki ; Imamura, Masayuki</creatorcontrib><description>BACKGROUND
Activation of matrix metalloproteinase‐2 (MMP‐2) has been implicated in the progression, invasion, and metastasis of various cancers, but little information is available with regard to its role in pancreatic carcinoma with poor prognosis.
METHODS
Gelatin zymography was used for the detection of latent and activated forms of MMP‐2 and MMP‐9 in 13 normal pancreatic tissue specimens, 14 chronic pancreatitis tissue specimens, and 33 pancreatic carcinoma tissue specimens. The gelatinase activity was quantified by densitometer, and the 66‐kilodalton (kDa)/(66‐kDa + 72‐kDa) ratio was calculated as the MMP‐2 activation ratio. Western blot analysis was performed to confirm the zymographic profile.
RESULTS
Latent forms of MMP‐2 and MMP‐9 were detected in all samples of pancreatic carcinoma, chronic pancreatitis, and normal pancreatic tissue. The expression rate of the MMP‐2 activated form in pancreatic carcinoma tissue specimens was 100% (33 of 33) but that of MMP‐9 was 21%. The MMP‐2 activation ratio in pancreatic carcinoma tissue specimens was significantly higher than that of chronic pancreatitis and normal pancreatic tissue specimens. The MMP‐2 activation ratio in pT3 tumors was significantly higher than that in pT1 tumors. The MMP‐2 activation ratio also was significantly higher in pancreatic carcinoma specimens with histologically positive regional lymph node metastasis and distant metastasis than those without metastasis. The MMP‐2 activation ratio observed in patients who developed postresection recurrence within 6 months was significantly higher than that in patients without recurrence at 6 months.
CONCLUSIONS
The results of the current study indicate that MMP‐2 activation plays a significant role in tumor invasion and metastasis in pancreatic carcinoma. Cancer 1998;82:642‐50. © 1998 American Cancer Society.
In this study, the activated form of matrix metalloproteinase‐2 (MMP‐2) was detected in pancreatic carcinoma, chronic pancreatitis, and normal pancreatic tissue specimens by zymographic analysis. The activation of MMP‐2 plays an important role in tumor invasion and metastasis in pancreatic carcinoma.</description><identifier>ISSN: 0008-543X</identifier><identifier>EISSN: 1097-0142</identifier><identifier>DOI: 10.1002/(SICI)1097-0142(19980215)82:4<642::AID-CNCR5>3.0.CO;2-N</identifier><identifier>PMID: 9477095</identifier><identifier>CODEN: CANCAR</identifier><language>eng</language><publisher>New York: John Wiley & Sons, Inc</publisher><subject>Adenocarcinoma, Mucinous - enzymology ; Adenocarcinoma, Mucinous - pathology ; Adenocarcinoma, Mucinous - secondary ; Aged ; Aged, 80 and over ; Biological and medical sciences ; Blotting, Western ; Collagenases - metabolism ; Electrophoresis, Polyacrylamide Gel ; Enzyme Activation ; Female ; Gastroenterology. Liver. Pancreas. Abdomen ; Gelatinases - metabolism ; Humans ; Liver. Biliary tract. Portal circulation. Exocrine pancreas ; Male ; Matrix Metalloproteinase 2 ; Matrix Metalloproteinase 9 ; Medical sciences ; Metalloendopeptidases - metabolism ; Middle Aged ; Neoplasm Invasiveness ; Pancreas ; Pancreas - enzymology ; Pancreas - pathology ; pancreatic carcinoma ; Pancreatic Neoplasms - enzymology ; Pancreatic Neoplasms - pathology ; Pancreatitis - enzymology ; Pancreatitis - pathology ; tissue ; Tumors ; Western blot analysis ; zymography</subject><ispartof>Cancer, 1998-02, Vol.82 (4), p.642-650</ispartof><rights>Copyright © 1998 American Cancer Society</rights><rights>1998 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><cites>FETCH-LOGICAL-c4755-180007e26aa79ac5aba38da5443e67708c22daef69e02b809ae7a7a0174498d13</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2F%28SICI%291097-0142%2819980215%2982%3A4%3C642%3A%3AAID-CNCR5%3E3.0.CO%3B2-N$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2F%28SICI%291097-0142%2819980215%2982%3A4%3C642%3A%3AAID-CNCR5%3E3.0.CO%3B2-N$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,776,780,1411,1427,27903,27904,45553,45554,46387,46811</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=2154934$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9477095$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Koshiba, Takatomo</creatorcontrib><creatorcontrib>Hosotani, Ryo</creatorcontrib><creatorcontrib>Wada, Michihiko</creatorcontrib><creatorcontrib>Miyamoto, Yoshiharu</creatorcontrib><creatorcontrib>Fujimoto, Koji</creatorcontrib><creatorcontrib>Lee, Jeon‐Uk</creatorcontrib><creatorcontrib>Doi, Ryuichiro</creatorcontrib><creatorcontrib>Arii, Shigeki</creatorcontrib><creatorcontrib>Imamura, Masayuki</creatorcontrib><title>Involvement of matrix metalloproteinase‐2 activity in invasion and metastasis of pancreatic carcinoma</title><title>Cancer</title><addtitle>Cancer</addtitle><description>BACKGROUND
Activation of matrix metalloproteinase‐2 (MMP‐2) has been implicated in the progression, invasion, and metastasis of various cancers, but little information is available with regard to its role in pancreatic carcinoma with poor prognosis.
METHODS
Gelatin zymography was used for the detection of latent and activated forms of MMP‐2 and MMP‐9 in 13 normal pancreatic tissue specimens, 14 chronic pancreatitis tissue specimens, and 33 pancreatic carcinoma tissue specimens. The gelatinase activity was quantified by densitometer, and the 66‐kilodalton (kDa)/(66‐kDa + 72‐kDa) ratio was calculated as the MMP‐2 activation ratio. Western blot analysis was performed to confirm the zymographic profile.
RESULTS
Latent forms of MMP‐2 and MMP‐9 were detected in all samples of pancreatic carcinoma, chronic pancreatitis, and normal pancreatic tissue. The expression rate of the MMP‐2 activated form in pancreatic carcinoma tissue specimens was 100% (33 of 33) but that of MMP‐9 was 21%. The MMP‐2 activation ratio in pancreatic carcinoma tissue specimens was significantly higher than that of chronic pancreatitis and normal pancreatic tissue specimens. The MMP‐2 activation ratio in pT3 tumors was significantly higher than that in pT1 tumors. The MMP‐2 activation ratio also was significantly higher in pancreatic carcinoma specimens with histologically positive regional lymph node metastasis and distant metastasis than those without metastasis. The MMP‐2 activation ratio observed in patients who developed postresection recurrence within 6 months was significantly higher than that in patients without recurrence at 6 months.
CONCLUSIONS
The results of the current study indicate that MMP‐2 activation plays a significant role in tumor invasion and metastasis in pancreatic carcinoma. Cancer 1998;82:642‐50. © 1998 American Cancer Society.
In this study, the activated form of matrix metalloproteinase‐2 (MMP‐2) was detected in pancreatic carcinoma, chronic pancreatitis, and normal pancreatic tissue specimens by zymographic analysis. The activation of MMP‐2 plays an important role in tumor invasion and metastasis in pancreatic carcinoma.</description><subject>Adenocarcinoma, Mucinous - enzymology</subject><subject>Adenocarcinoma, Mucinous - pathology</subject><subject>Adenocarcinoma, Mucinous - secondary</subject><subject>Aged</subject><subject>Aged, 80 and over</subject><subject>Biological and medical sciences</subject><subject>Blotting, Western</subject><subject>Collagenases - metabolism</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Enzyme Activation</subject><subject>Female</subject><subject>Gastroenterology. Liver. Pancreas. Abdomen</subject><subject>Gelatinases - metabolism</subject><subject>Humans</subject><subject>Liver. Biliary tract. Portal circulation. Exocrine pancreas</subject><subject>Male</subject><subject>Matrix Metalloproteinase 2</subject><subject>Matrix Metalloproteinase 9</subject><subject>Medical sciences</subject><subject>Metalloendopeptidases - metabolism</subject><subject>Middle Aged</subject><subject>Neoplasm Invasiveness</subject><subject>Pancreas</subject><subject>Pancreas - enzymology</subject><subject>Pancreas - pathology</subject><subject>pancreatic carcinoma</subject><subject>Pancreatic Neoplasms - enzymology</subject><subject>Pancreatic Neoplasms - pathology</subject><subject>Pancreatitis - enzymology</subject><subject>Pancreatitis - pathology</subject><subject>tissue</subject><subject>Tumors</subject><subject>Western blot analysis</subject><subject>zymography</subject><issn>0008-543X</issn><issn>1097-0142</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1998</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkd1q2zAYhsXY6NJulzDwwRjtgTNJliwrGy3F-zOUBPbDevbxRZaHhn9Sy8mWs11Cr7FXMrnJcrLBQCCk79Wrh_cl5ILRKaOUvzz9VOTFGaNaxZQJfsq0zihn8izjM_E6FXw2uyzexPk8_yjPkymd5otXPJ4_IJPDm4dkQinNYimS68fk2Pvv4ai4TI7IkRZKUS0n5FvRbrp6YxvbDlFXRQ0OvfsZNXbAuu5WfTdY16K3d79ueYRmcBs3bCPXhrVB77o2wra8l_uwnB89Vtia3uLgTGSwN67tGnxCHlVYe_t0v5-QL-_efs4_xFeL90V-eRUboaSMWTYyWp4iKo1G4hKTrEQpRGLTgJwZzku0Vaot5cuMarQKFVKmhNBZyZIT8mLnG9Bv1tYP0DhvbF1ja7u1B6VTLaQWQfh1JzR9531vK1j1rsF-C4zCWAHAWAGMccIYJ_ypADIOAkIFAKECuK8AEqCQL4DDPDg_2yOsl40tD777zMP8-X6O3mBd9SEu5w-y8IPQyQh4vZP9cLXd_kX3X7h_se0ukt-41LFY</recordid><startdate>19980215</startdate><enddate>19980215</enddate><creator>Koshiba, Takatomo</creator><creator>Hosotani, Ryo</creator><creator>Wada, Michihiko</creator><creator>Miyamoto, Yoshiharu</creator><creator>Fujimoto, Koji</creator><creator>Lee, Jeon‐Uk</creator><creator>Doi, Ryuichiro</creator><creator>Arii, Shigeki</creator><creator>Imamura, Masayuki</creator><general>John Wiley & Sons, Inc</general><general>Wiley-Liss</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>7X8</scope></search><sort><creationdate>19980215</creationdate><title>Involvement of matrix metalloproteinase‐2 activity in invasion and metastasis of pancreatic carcinoma</title><author>Koshiba, Takatomo ; Hosotani, Ryo ; Wada, Michihiko ; Miyamoto, Yoshiharu ; Fujimoto, Koji ; Lee, Jeon‐Uk ; Doi, Ryuichiro ; Arii, Shigeki ; Imamura, Masayuki</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4755-180007e26aa79ac5aba38da5443e67708c22daef69e02b809ae7a7a0174498d13</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1998</creationdate><topic>Adenocarcinoma, Mucinous - enzymology</topic><topic>Adenocarcinoma, Mucinous - pathology</topic><topic>Adenocarcinoma, Mucinous - secondary</topic><topic>Aged</topic><topic>Aged, 80 and over</topic><topic>Biological and medical sciences</topic><topic>Blotting, Western</topic><topic>Collagenases - metabolism</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Enzyme Activation</topic><topic>Female</topic><topic>Gastroenterology. Liver. Pancreas. Abdomen</topic><topic>Gelatinases - metabolism</topic><topic>Humans</topic><topic>Liver. Biliary tract. Portal circulation. Exocrine pancreas</topic><topic>Male</topic><topic>Matrix Metalloproteinase 2</topic><topic>Matrix Metalloproteinase 9</topic><topic>Medical sciences</topic><topic>Metalloendopeptidases - metabolism</topic><topic>Middle Aged</topic><topic>Neoplasm Invasiveness</topic><topic>Pancreas</topic><topic>Pancreas - enzymology</topic><topic>Pancreas - pathology</topic><topic>pancreatic carcinoma</topic><topic>Pancreatic Neoplasms - enzymology</topic><topic>Pancreatic Neoplasms - pathology</topic><topic>Pancreatitis - enzymology</topic><topic>Pancreatitis - pathology</topic><topic>tissue</topic><topic>Tumors</topic><topic>Western blot analysis</topic><topic>zymography</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Koshiba, Takatomo</creatorcontrib><creatorcontrib>Hosotani, Ryo</creatorcontrib><creatorcontrib>Wada, Michihiko</creatorcontrib><creatorcontrib>Miyamoto, Yoshiharu</creatorcontrib><creatorcontrib>Fujimoto, Koji</creatorcontrib><creatorcontrib>Lee, Jeon‐Uk</creatorcontrib><creatorcontrib>Doi, Ryuichiro</creatorcontrib><creatorcontrib>Arii, Shigeki</creatorcontrib><creatorcontrib>Imamura, Masayuki</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>MEDLINE - Academic</collection><jtitle>Cancer</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Koshiba, Takatomo</au><au>Hosotani, Ryo</au><au>Wada, Michihiko</au><au>Miyamoto, Yoshiharu</au><au>Fujimoto, Koji</au><au>Lee, Jeon‐Uk</au><au>Doi, Ryuichiro</au><au>Arii, Shigeki</au><au>Imamura, Masayuki</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Involvement of matrix metalloproteinase‐2 activity in invasion and metastasis of pancreatic carcinoma</atitle><jtitle>Cancer</jtitle><addtitle>Cancer</addtitle><date>1998-02-15</date><risdate>1998</risdate><volume>82</volume><issue>4</issue><spage>642</spage><epage>650</epage><pages>642-650</pages><issn>0008-543X</issn><eissn>1097-0142</eissn><coden>CANCAR</coden><abstract>BACKGROUND
Activation of matrix metalloproteinase‐2 (MMP‐2) has been implicated in the progression, invasion, and metastasis of various cancers, but little information is available with regard to its role in pancreatic carcinoma with poor prognosis.
METHODS
Gelatin zymography was used for the detection of latent and activated forms of MMP‐2 and MMP‐9 in 13 normal pancreatic tissue specimens, 14 chronic pancreatitis tissue specimens, and 33 pancreatic carcinoma tissue specimens. The gelatinase activity was quantified by densitometer, and the 66‐kilodalton (kDa)/(66‐kDa + 72‐kDa) ratio was calculated as the MMP‐2 activation ratio. Western blot analysis was performed to confirm the zymographic profile.
RESULTS
Latent forms of MMP‐2 and MMP‐9 were detected in all samples of pancreatic carcinoma, chronic pancreatitis, and normal pancreatic tissue. The expression rate of the MMP‐2 activated form in pancreatic carcinoma tissue specimens was 100% (33 of 33) but that of MMP‐9 was 21%. The MMP‐2 activation ratio in pancreatic carcinoma tissue specimens was significantly higher than that of chronic pancreatitis and normal pancreatic tissue specimens. The MMP‐2 activation ratio in pT3 tumors was significantly higher than that in pT1 tumors. The MMP‐2 activation ratio also was significantly higher in pancreatic carcinoma specimens with histologically positive regional lymph node metastasis and distant metastasis than those without metastasis. The MMP‐2 activation ratio observed in patients who developed postresection recurrence within 6 months was significantly higher than that in patients without recurrence at 6 months.
CONCLUSIONS
The results of the current study indicate that MMP‐2 activation plays a significant role in tumor invasion and metastasis in pancreatic carcinoma. Cancer 1998;82:642‐50. © 1998 American Cancer Society.
In this study, the activated form of matrix metalloproteinase‐2 (MMP‐2) was detected in pancreatic carcinoma, chronic pancreatitis, and normal pancreatic tissue specimens by zymographic analysis. The activation of MMP‐2 plays an important role in tumor invasion and metastasis in pancreatic carcinoma.</abstract><cop>New York</cop><pub>John Wiley & Sons, Inc</pub><pmid>9477095</pmid><doi>10.1002/(SICI)1097-0142(19980215)82:4<642::AID-CNCR5>3.0.CO;2-N</doi><tpages>9</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Adenocarcinoma, Mucinous - enzymology Adenocarcinoma, Mucinous - pathology Adenocarcinoma, Mucinous - secondary Aged Aged, 80 and over Biological and medical sciences Blotting, Western Collagenases - metabolism Electrophoresis, Polyacrylamide Gel Enzyme Activation Female Gastroenterology. Liver. Pancreas. Abdomen Gelatinases - metabolism Humans Liver. Biliary tract. Portal circulation. Exocrine pancreas Male Matrix Metalloproteinase 2 Matrix Metalloproteinase 9 Medical sciences Metalloendopeptidases - metabolism Middle Aged Neoplasm Invasiveness Pancreas Pancreas - enzymology Pancreas - pathology pancreatic carcinoma Pancreatic Neoplasms - enzymology Pancreatic Neoplasms - pathology Pancreatitis - enzymology Pancreatitis - pathology tissue Tumors Western blot analysis zymography |
| title | Involvement of matrix metalloproteinase‐2 activity in invasion and metastasis of pancreatic carcinoma |
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