KLK7 expression in human tumors: a tissue microarray study on 13,447 tumors.
Immunohistochemistry
KLK7
Neoplastic human tissues
Tissue microarray
Journal
BMC cancer
ISSN: 1471-2407
Titre abrégé: BMC Cancer
Pays: England
ID NLM: 100967800
Informations de publication
Date de publication:
03 Jul 2024
03 Jul 2024
Historique:
received:
26
10
2022
accepted:
23
06
2024
medline:
4
7
2024
pubmed:
4
7
2024
entrez:
3
7
2024
Statut:
epublish
Résumé
Kallikrein-related peptidase 7 (KLK7) is a chymotrypsin-like serine protease which is essential for the desquamation of corneocytes and thus plays a pivotal role in maintaining skin homeostasis. In cancer, KLK7 overexpression was suggested to represent a route for metastasis through cleavage of cell junction and extracellular matrix proteins of cancer cells. To comprehensively determine KLK7 protein expression in normal and neoplastic tissues, a tissue microarray containing 13,447 samples from 147 different tumor types and subtypes as well as 608 samples of 76 different normal tissue types was analyzed by immunohistochemistry. KLK7 positivity was found in 64 of 147 tumor categories, including 17 tumor categories with at least one strongly positive case. The highest rate of KLK7 positivity was found in squamous cell carcinomas from various sites of origin (positive in 18.1%-63.8%), ovarian and endometrium cancers (4.8%-56.2%), salivary gland tumors (4.8%-13.7%), bilio-pancreatic adenocarcinomas (20.0%-40.4%), and adenocarcinomas of the upper gastrointestinal tract (3.3%-12.5%). KLK7 positivity was linked to nodal metastasis (p = 0.0005), blood vessel infiltration (p = 0.0037), and lymph vessel infiltration (p < 0.0001) in colorectal adenocarcinoma, nodal metastasis in hepatocellular carcinoma (p = 0.0382), advanced pathological tumor stage in papillary thyroid cancer (p = 0.0132), and low grade of malignancy in a cohort of 719 squamous cell carcinomas from 11 different sites of origin (p < 0.0001). These data provide a comprehensive overview on KLK7 expression in normal and neoplastic human tissues. The prognostic relevance of KLK7 expression and the possible role of KLK7 as a drug target need to be further investigated.
Sections du résumé
BACKGROUND
BACKGROUND
Kallikrein-related peptidase 7 (KLK7) is a chymotrypsin-like serine protease which is essential for the desquamation of corneocytes and thus plays a pivotal role in maintaining skin homeostasis. In cancer, KLK7 overexpression was suggested to represent a route for metastasis through cleavage of cell junction and extracellular matrix proteins of cancer cells.
METHODS
METHODS
To comprehensively determine KLK7 protein expression in normal and neoplastic tissues, a tissue microarray containing 13,447 samples from 147 different tumor types and subtypes as well as 608 samples of 76 different normal tissue types was analyzed by immunohistochemistry.
RESULTS
RESULTS
KLK7 positivity was found in 64 of 147 tumor categories, including 17 tumor categories with at least one strongly positive case. The highest rate of KLK7 positivity was found in squamous cell carcinomas from various sites of origin (positive in 18.1%-63.8%), ovarian and endometrium cancers (4.8%-56.2%), salivary gland tumors (4.8%-13.7%), bilio-pancreatic adenocarcinomas (20.0%-40.4%), and adenocarcinomas of the upper gastrointestinal tract (3.3%-12.5%). KLK7 positivity was linked to nodal metastasis (p = 0.0005), blood vessel infiltration (p = 0.0037), and lymph vessel infiltration (p < 0.0001) in colorectal adenocarcinoma, nodal metastasis in hepatocellular carcinoma (p = 0.0382), advanced pathological tumor stage in papillary thyroid cancer (p = 0.0132), and low grade of malignancy in a cohort of 719 squamous cell carcinomas from 11 different sites of origin (p < 0.0001).
CONCLUSIONS
CONCLUSIONS
These data provide a comprehensive overview on KLK7 expression in normal and neoplastic human tissues. The prognostic relevance of KLK7 expression and the possible role of KLK7 as a drug target need to be further investigated.
Identifiants
pubmed: 38961454
doi: 10.1186/s12885-024-12552-8
pii: 10.1186/s12885-024-12552-8
doi:
Substances chimiques
Kallikreins
EC 3.4.21.-
KLK7 protein, human
EC 3.4.21.-
Biomarkers, Tumor
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
794Informations de copyright
© 2024. The Author(s).
Références
Clements J, Hooper J, Dong Y, Harvey T. The expanded human kallikrein (KLK) gene family: genomic organisation, tissue-specific expression and potential functions. Biol Chem. 2001;382(1):5–14.
pubmed: 11258672
doi: 10.1515/BC.2001.002
Hong SK. Kallikreins as biomarkers for prostate cancer. Biomed Res Int. 2014;2014:526341.
pubmed: 24809052
pmcid: 3997884
doi: 10.1155/2014/526341
Avgeris M, Mavridis K, Scorilas A. Kallikrein-related peptidases in prostate, breast, and ovarian cancers: from pathobiology to clinical relevance. Biol Chem. 2012;393(5):301–17.
pubmed: 22505514
doi: 10.1515/hsz-2011-0260
Yousef GM, Scorilas A, Magklara A, Soosaipillai A, Diamandis EP. The KLK7 (PRSS6) gene, encoding for the stratum corneum chymotryptic enzyme is a new member of the human kallikrein gene family - genomic characterization, mapping, tissue expression and hormonal regulation. Gene. 2000;254(1–2):119–28.
pubmed: 10974542
doi: 10.1016/S0378-1119(00)00280-8
Caubet C, Jonca N, Brattsand M, Guerrin M, Bernard D, Schmidt R, Egelrud T, Simon M, Serre G. Degradation of corneodesmosome proteins by two serine proteases of the kallikrein family, SCTE/KLK5/hK5 and SCCE/KLK7/hK7. J Invest Dermatol. 2004;122(5):1235–44.
pubmed: 15140227
doi: 10.1111/j.0022-202X.2004.22512.x
de Veer SJ, Furio L, Swedberg JE, Munro CA, Brattsand M, Clements JA, Hovnanian A, Harris JM. Selective Substrates and Inhibitors for Kallikrein-Related Peptidase 7 (KLK7) Shed Light on KLK Proteolytic Activity in the Stratum Corneum. J Invest Dermatol. 2017;137(2):430–9.
pubmed: 27697464
doi: 10.1016/j.jid.2016.09.017
Hansson L, Strömqvist M, Bäckman A, Wallbrandt P, Carlstein A, Egelrud T. Cloning, expression, and characterization of stratum corneum chymotryptic enzyme. A skin-specific human serine proteinase. J Biol Chem. 1994;269(30):19420–6.
pubmed: 8034709
doi: 10.1016/S0021-9258(17)32185-3
Levi K, Baxter J, Meldrum H, Misra M, Pashkovski E, Dauskardt RH. Effect of corneodesmosome degradation on the intercellular delamination of human stratum corneum. J Invest Dermatol. 2008;128(9):2345–7.
pubmed: 18449214
doi: 10.1038/jid.2008.107
Kishibe M. Physiological and pathological roles of kallikrein-related peptidases in the epidermis. J Dermatol Sci. 2019;95(2):50–5.
pubmed: 31279501
doi: 10.1016/j.jdermsci.2019.06.007
Iakovlev V, Siegel ER, Tsao MS, Haun RS. Expression of kallikrein-related peptidase 7 predicts poor prognosis in patients with unresectable pancreatic ductal adenocarcinoma. Cancer Epidemiol Biomarkers Prev. 2012;21(7):1135–42.
pubmed: 22573795
doi: 10.1158/1055-9965.EPI-11-1079
Johnson SK, Ramani VC, Hennings L, Haun RS. Kallikrein 7 enhances pancreatic cancer cell invasion by shedding E-cadherin. Cancer. 2007;109(9):1811–20.
pubmed: 17354228
doi: 10.1002/cncr.22606
Shigemasa K, Tanimoto H, Underwood LJ, Parmley TH, Arihiro K, Ohama K, O’Brien TJ. Expression of the protease inhibitor antileukoprotease and the serine protease stratum corneum chymotryptic enzyme (SCCE) is coordinated in ovarian tumors. Int J Gynecol Cancer. 2001;11(6):454–61.
pubmed: 11906548
doi: 10.1136/ijgc-00009577-200111000-00005
Wang P, Magdolen V, Seidl C, Dorn J, Drecoll E, Kotzsch M, Yang F, Schmitt M, Schilling O, Rockstroh A, et al. Kallikrein-related peptidases 4, 5, 6 and 7 regulate tumour-associated factors in serous ovarian cancer. Br J Cancer. 2018;119(7):1–9.
pubmed: 30287916
pmcid: 6189062
doi: 10.1038/s41416-018-0260-1
Dorn J, Gkazepis A, Kotzsch M, Kremer M, Propping C, Mayer K, Mengele K, Diamandis EP, Kiechle M, Magdolen V, et al. Clinical value of protein expression of kallikrein-related peptidase 7 (KLK7) in ovarian cancer. Biol Chem. 2014;395(1):95–107.
pubmed: 23999494
doi: 10.1515/hsz-2013-0172
Xuan Q, Yang X, Mo L, Huang F, Pang Y, Qin M, Chen Z, He M, Wang Q, Mo ZN. Expression of the serine protease kallikrein 7 and its inhibitor antileukoprotease is decreased in prostate cancer. Arch Pathol Lab Med. 2008;132(11):1796–801.
pubmed: 18976018
doi: 10.5858/132.11.1796
Zhang CY, Zhu Y, Rui WB, Dai J, Shen ZJ. Expression of kallikrein-related peptidase 7 is decreased in prostate cancer. Asian J Androl. 2015;17(1):106–10.
pubmed: 25219913
doi: 10.1002/asia.201402962
Geng X, Babayeva L, Walch A, Aubele M, Groß E, Kiechle M, Bronger H, Dreyer T, Magdolen V, Dorn J. High levels of KLK7 protein expression are related to a favorable prognosis in triple-negative breast cancer patients. Am J Cancer Res. 2020;10(6):1785–92.
pubmed: 32642290
pmcid: 7339269
Santin AD, Cane’ S, Bellone S, Bignotti E, Palmieri M, De Las Casas LE, Roman JJ, Anfossi S, O’Brien T, Pecorelli S. The serine protease stratum corneum chymotryptic enzyme (kallikrein 7) is highly overexpressed in squamous cervical cancer cells. Gynecol Oncol. 2004;94(2):283–8.
pubmed: 15297163
doi: 10.1016/j.ygyno.2004.05.023
Delaunay T, Deschamps L, Haddada M, Walker F, Soosaipillai A, Soualmia F, El Amri C, Diamandis EP, Brattsand M, Magdolen V, et al. Aberrant expression of kallikrein-related peptidase 7 is correlated with human melanoma aggressiveness by stimulating cell migration and invasion. Mol Oncol. 2017;11(10):1330–47.
pubmed: 28636767
pmcid: 5623816
doi: 10.1002/1878-0261.12103
Kumar DV, Sivaranjani Y, Rao GV. Immunohistochemical expression of kallikrein 7 in oral squamous cell carcinoma. J Oral Maxillofac Pathol. 2020;24(3):580.
pubmed: 33967508
doi: 10.4103/jomfp.JOMFP_244_19
Walker F, Nicole P, Jallane A, Soosaipillai A, Mosbach V, Oikonomopoulou K, Diamandis EP, Magdolen V, Darmoul D. Kallikrein-related peptidase 7 (KLK7) is a proliferative factor that is aberrantly expressed in human colon cancer. Biol Chem. 2014;395(9):1075–86.
pubmed: 25153388
doi: 10.1515/hsz-2014-0142
Pettus JR, Johnson JJ, Shi Z, Davis JW, Koblinski J, Ghosh S, Liu Y, Ravosa MJ, Frazier S, Stack MS. Multiple kallikrein (KLK 5, 7, 8, and 10) expression in squamous cell carcinoma of the oral cavity. Histol Histopathol. 2009;24(2):197–207.
pubmed: 19085836
pmcid: 2835693
Termini L, Maciag PC, Soares FA, Nonogaki S, Pereira SM, Alves VA, Longatto-Filho A, Villa LL. Analysis of human kallikrein 7 expression as a potential biomarker in cervical neoplasia. Int J Cancer. 2010;127(2):485–90.
pubmed: 19921697
doi: 10.1002/ijc.25046
Tian X, Shigemasa K, Hirata E, Gu L, Uebaba Y, Nagai N, O’Brien TJ, Ohama K. Expression of human kallikrein 7 (hK7/SCCE) and its inhibitor antileukoprotease (ALP/SLPI) in uterine endocervical glands and in cervical adenocarcinomas. Oncol Rep. 2004;12(5):1001–6.
pubmed: 15492784
Zhao H, Dong Y, Quan J, Smith R, Lam A, Weinstein S, Clements J, Johnson NW, Gao J. Correlation of the expression of human kallikrein-related peptidases 4 and 7 with the prognosis in oral squamous cell carcinoma. Head Neck. 2011;33(4):566–72.
pubmed: 20665732
doi: 10.1002/hed.21496
Leusink FK, van Diest PJ, Frank MH, Broekhuizen R, Braunius W, van Hooff SR, Willems SM, Koole R. The Co-Expression of Kallikrein 5 and Kallikrein 7 Associates with Poor Survival in Non-HPV Oral Squamous-Cell Carcinoma. Pathobiology. 2015;82(2):58–67.
pubmed: 26022646
doi: 10.1159/000381904
Gabril M, White NM, Moussa M, Chow TF, Metias SM, Fatoohi E, Yousef GM. Immunohistochemical analysis of kallikrein-related peptidases in the normal kidney and renal tumors: potential clinical implications. Biol Chem. 2010;391(4):403–9.
pubmed: 20128686
doi: 10.1515/bc.2010.025
Xiang F, Wang Y, Cao C, Li Q, Deng H, Zheng J, Liu X, Tan X. The Role of Kallikrein 7 in Tumorigenesis. Curr Med Chem. 2022;29(15):2617–31.
pubmed: 34525904
doi: 10.2174/0929867328666210915104537
Rico SD, Mahnken M, Buscheck F, Dum D, Luebke AM, Kluth M, Hube-Magg C, Hinsch A, Hoflmayer D, Moller-Koop C, et al. MUC5AC Expression in Various Tumor Types and Nonneoplastic Tissue: A Tissue Microarray Study on 10 399 Tissue Samples. Technol Cancer Res Treat. 2021;20:15330338211043328.
pubmed: 34547930
pmcid: 8461123
doi: 10.1177/15330338211043328
Steurer S, Riemann C, Buscheck F, Luebke AM, Kluth M, Hube-Magg C, Hinsch A, Hoflmayer D, Weidemann S, Fraune C, et al. p63 expression in human tumors and normal tissues: a tissue microarray study on 10,200 tumors. Biomark Res. 2021;9(1):7.
pubmed: 33494829
pmcid: 7830855
doi: 10.1186/s40364-021-00260-5
Uhlig R, Gunther K, Broker N, Gorbokon N, Lennartz M, Dwertmann Rico S, Reiswich V, Viehweger F, Buscheck F, Kluth M, et al. Diagnostic and prognostic role of pancreatic secretory granule membrane major glycoprotein 2 (GP2) immunohistochemistry: A TMA study on 27,681 tumors. Pathol Res Pract. 2022;238:154123.
pubmed: 36137400
doi: 10.1016/j.prp.2022.154123
Bubendorf L, Nocito A, Moch H, Sauter G. Tissue microarray (TMA) technology: miniaturized pathology archives for high-throughput in situ studies. J Pathol. 2001;195(1):72–9.
pubmed: 11568893
doi: 10.1002/path.893
Kononen J, Bubendorf L, Kallioniemi A, Bärlund M, Schraml P, Leighton S, Torhorst J, Mihatsch MJ, Sauter G, Kallioniemi OP. Tissue microarrays for high-throughput molecular profiling of tumor specimens. Nat Med. 1998;4(7):844–7.
pubmed: 9662379
doi: 10.1038/nm0798-844
Uhlen M, Bandrowski A, Carr S, Edwards A, Ellenberg J, Lundberg E, Rimm DL, Rodriguez H, Hiltke T, Snyder M, et al. A proposal for validation of antibodies. Nat Methods. 2016;13(10):823–7.
pubmed: 27595404
pmcid: 10335836
doi: 10.1038/nmeth.3995
Lizio M, Harshbarger J, Shimoji H, Severin J, Kasukawa T, Sahin S, Abugessaisa I, Fukuda S, Hori F, Ishikawa-Kato S, et al. Gateways to the FANTOM5 promoter level mammalian expression atlas. Genome Biol. 2015;16:22.
pubmed: 25723102
pmcid: 4310165
doi: 10.1186/s13059-014-0560-6
Lizio M, Harshbarger J, Abugessaisa I, Noguchi S, Kondo A, Severin J, Mungall C, Arenillas D, Mathelier A, Medvedeva YA, et al. Update of the FANTOM web resource: high resolution transcriptome of diverse cell types in mammals. Nucleic Acids Res. 2017;45(D1):D737–43.
pubmed: 27794045
doi: 10.1093/nar/gkw995
Consortium G. The Genotype-Tissue Expression (GTEx) project. Nat Genet. 2013;45(6):580–5.
doi: 10.1038/ng.2653
Karlsson M, Zhang C, Méar L, Zhong W, Digre A, Katona B, Sjöstedt E, Butler L, Odeberg J, Dusart P, et al. A single-cell type transcriptomics map of human tissues. Sci Adv. 2021;7(31):eabh2169.
pubmed: 34321199
pmcid: 8318366
doi: 10.1126/sciadv.abh2169
Yousef GM, Yacoub GM, Polymeris ME, Popalis C, Soosaipillai A, Diamandis EP. Kallikrein gene downregulation in breast cancer. Br J Cancer. 2004;90(1):167–72.
pubmed: 14710225
pmcid: 2395319
doi: 10.1038/sj.bjc.6601451
Li X, Liu J, Wang Y, Zhang L, Ning L, Feng Y. Parallel underexpression of kallikrein 5 and kallikrein 7 mRNA in breast malignancies. Cancer Sci. 2009;100(4):601–7.
pubmed: 19453546
pmcid: 11158435
doi: 10.1111/j.1349-7006.2009.01090.x
Talieri M, Diamandis EP, Gourgiotis D, Mathioudaki K, Scorilas A. Expression analysis of the human kallikrein 7 (KLK7) in breast tumors: a new potential biomarker for prognosis of breast carcinoma. Thromb Haemost. 2004;91(1):180–6.
pubmed: 14691584
doi: 10.1160/TH03-05-0261
Cerami E, Gao J, Dogrusoz U, Gross BE, Sumer SO, Aksoy BA, Jacobsen A, Byrne CJ, Heuer ML, Larsson E, et al. The cBio cancer genomics portal: an open platform for exploring multidimensional cancer genomics data. Cancer Discov. 2012;2(5):401–4.
pubmed: 22588877
doi: 10.1158/2159-8290.CD-12-0095
Gao J, Aksoy BA, Dogrusoz U, Dresdner G, Gross B, Sumer SO, Sun Y, Jacobsen A, Sinha R, Larsson E, et al. Integrative analysis of complex cancer genomics and clinical profiles using the cBioPortal. Sci Signal. 2013;6(269):pl1.
pubmed: 23550210
pmcid: 4160307
doi: 10.1126/scisignal.2004088
Okegawa T, Pong RC, Li Y, Hsieh JT. The role of cell adhesion molecule in cancer progression and its application in cancer therapy. Acta Biochim Pol. 2004;51(2):445–57.
pubmed: 15218541
doi: 10.18388/abp.2004_3583
Kramer IR, Lucas RB, Pindborg JJ, Sobin LH. Definition of leukoplakia and related lesions: an aid to studies on oral precancer. Oral Surg Oral Med Oral Pathol. 1978;46(4):518–39.
pubmed: 280847
doi: 10.1016/0030-4220(78)90383-3
van Harten AM, Brakenhoff RH. Targeted Treatment of Head and Neck (Pre) Cancer: Preclinical Target Identification and Development of Novel Therapeutic Applications. Cancers (Basel). 2021;13(11):2774.
pubmed: 34204886
doi: 10.3390/cancers13112774
Taggart MW, Rashid A, Ross WA, Abraham SC. Oesophageal hyperkeratosis: clinicopathological associations. Histopathology. 2013;63(4):463–73.
pubmed: 23879628
doi: 10.1111/his.12195
Travis WD, Brambilla E, Nicholson AG, Yatabe Y, Austin JHM, Beasley MB, Chirieac LR, Dacic S, Duhig E, Flieder DB, et al. The 2015 World Health Organization Classification of Lung Tumors: Impact of Genetic, Clinical and Radiologic Advances Since the 2004 Classification. J Thorac Oncol. 2015;10(9):1243–60.
pubmed: 26291008
doi: 10.1097/JTO.0000000000000630
Uhlig R, Abboud M, Gorbokon N, Lennartz M, Dwertmann Rico S, Kind S, Reiswich V, Viehweger F, Kluth M, Hube-Magg C, et al. Cytokeratin 10 (CK10) expression in cancer: A tissue microarray study on 11,021 tumors. Ann Diagn Pathol. 2022;60:152029.
pubmed: 36029589
doi: 10.1016/j.anndiagpath.2022.152029
Silva LM, Kryza T, Stoll T, Hoogland C, Dong Y, Stephens CR, Hastie ML, Magdolen V, Kleifeld O, Gorman JJ, et al. Integration of Two In-depth Quantitative Proteomics Approaches Determines the Kallikrein-related Peptidase 7 (KLK7) Degradome in Ovarian Cancer Cell Secretome. Mol Cell Proteomics. 2019;18(5):818–36.
pubmed: 30705123
pmcid: 6495248
doi: 10.1074/mcp.RA118.001304
Ramani VC, Hennings L, Haun RS. Desmoglein 2 is a substrate of kallikrein 7 in pancreatic cancer. BMC Cancer. 2008;8:373.
pubmed: 19091121
pmcid: 2628383
doi: 10.1186/1471-2407-8-373
Yu Y, Prassas I, Dimitromanolakis A, Diamandis EP. Novel Biological Substrates of Human Kallikrein 7 Identified through Degradomics. J Biol Chem. 2015;290(29):17762–75.
pubmed: 26032414
pmcid: 4505025
doi: 10.1074/jbc.M115.643551
Ramani VC, Haun RS. Expression of kallikrein 7 diminishes pancreatic cancer cell adhesion to vitronectin and enhances urokinase-type plasminogen activator receptor shedding. Pancreas. 2008;37(4):399–404.
pubmed: 18953252
doi: 10.1097/MPA.0b013e31817f76f7
Mo L, Zhang J, Shi J, Xuan Q, Yang X, Qin M, Lee C, Klocker H, Li QQ, Mo Z. Human kallikrein 7 induces epithelial-mesenchymal transition-like changes in prostate carcinoma cells: a role in prostate cancer invasion and progression. Anticancer Res. 2010;30(9):3413–20.
pubmed: 20944116
Ramani VC, Haun RS. The extracellular matrix protein fibronectin is a substrate for kallikrein 7. Biochem Biophys Res Commun. 2008;369(4):1169–73.
pubmed: 18343220
doi: 10.1016/j.bbrc.2008.03.021
Wong SHM, Fang CM, Chuah LH, Leong CO, Ngai SC. E-cadherin: Its dysregulation in carcinogenesis and clinical implications. Crit Rev Oncol Hematol. 2018;121:11–22.
pubmed: 29279096
doi: 10.1016/j.critrevonc.2017.11.010
Bazzazi H, Zhang Y, Jafarnejad M, Isenberg JS, Annex BH, Popel AS. Computer Simulation of TSP1 Inhibition of VEGF-Akt-eNOS: An Angiogenesis Triple Threat. Front Physiol. 2018;9:644.
pubmed: 29899706
pmcid: 5988849
doi: 10.3389/fphys.2018.00644
Bussolati B, Assenzio B, Deregibus MC, Camussi G. The proangiogenic phenotype of human tumor-derived endothelial cells depends on thrombospondin-1 downregulation via phosphatidylinositol 3-kinase/Akt pathway. J Mol Med (Berl). 2006;84(10):852–63.
pubmed: 16924472
doi: 10.1007/s00109-006-0075-z
Bach LA. What Happened to the IGF Binding Proteins? Endocrinology. 2018;159(2):570–8.
pubmed: 29165552
doi: 10.1210/en.2017-00908
Hoxhaj G, Manning BD. The PI3K-AKT network at the interface of oncogenic signalling and cancer metabolism. Nat Rev Cancer. 2020;20(2):74–88.
pubmed: 31686003
doi: 10.1038/s41568-019-0216-7
Ramani VC, Kaushal GP, Haun RS. Proteolytic action of kallikrein-related peptidase 7 produces unique active matrix metalloproteinase-9 lacking the C-terminal hemopexin domains. Biochim Biophys Acta. 2011;1813(8):1525–31.
pubmed: 21616098
pmcid: 3123393
doi: 10.1016/j.bbamcr.2011.05.007
Davidson B, Reich R, Risberg B, Nesland JM. The biological role and regulation of matrix metalloproteinases (MMP) in cancer. Arkh Patol. 2002;64(3):47–53.
pubmed: 15338725
Sauter G. Representativity of TMA studies. Methods Mol Biol. 2010;664:27–35.
pubmed: 20690049
doi: 10.1007/978-1-60761-806-5_3
Torhorst J, Bucher C, Kononen J, Haas P, Zuber M, Kochli OR, Mross F, Dieterich H, Moch H, Mihatsch M, et al. Tissue microarrays for rapid linking of molecular changes to clinical endpoints. Am J Pathol. 2001;159(6):2249–56.
pubmed: 11733374
pmcid: 1850582
doi: 10.1016/S0002-9440(10)63075-1
Du JP, Li L, Zheng J, Zhang D, Liu W, Zheng WH, Li XS, Yao RC, Wang F, Liu S, et al. Kallikrein-related peptidase 7 is a potential target for the treatment of pancreatic cancer. Oncotarget. 2018;9(16):12894–906.
pubmed: 29560118
pmcid: 5849182
doi: 10.18632/oncotarget.24132