|
1
|
Carne PW, Frye JN, Robertson GM and
Frizelle FA: Parastomal hernia following minimally invasive stoma
formation. ANZ J Surg. 73:843–845. 2003. View Article : Google Scholar : PubMed/NCBI
|
|
2
|
Celik S, Firat Kocaay A and Akyol C:
Parastomal Hernia. pp. 185–199. 2017, http://dx.doi.org/10.5772/intechopen.68876Accessed
August 30, 2017.
|
|
3
|
van Dijk SM, Timmermans L, Deerenberg EB,
Lamme B, Kleinrensink GJ, Jeekel J and Lange JF: Parastomal hernia:
Impact on quality of life? . World J Surg. 39:2595–2601. 2015.
View Article : Google Scholar : PubMed/NCBI
|
|
4
|
Kwiatt M and Kawata M: Avoidance and
management of stomal complications. Clin Colon Rectal Surg.
26:112–121. 2013. View Article : Google Scholar :
|
|
5
|
Shah NR, Craft RO and Harold KL:
Parastomal hernia repair. Surg Clin North Am. 93:1185–1198. 2013.
View Article : Google Scholar : PubMed/NCBI
|
|
6
|
Sohn YJ, Moon SM, Shin US and Jee SH:
Incidence and risk factors of parastomal hernia. J Korean Soc
Coloproctol. 28:241–246. 2012. View Article : Google Scholar : PubMed/NCBI
|
|
7
|
Hong SY, Oh SY, Lee JH, Kim DY and Suh KW:
Risk factors for parastomal hernia: Based on radiological
definition. J Korean Surg Soc. 84:43–47. 2013. View Article : Google Scholar : PubMed/NCBI
|
|
8
|
Skibiński R, Pasternak A, Szura M, Solecki
R, Matyja M and Matyja A: Parastomal hernia-contemporary methods of
treatment. Pol Przegl Chir. 87:531–537. 2015. View Article : Google Scholar
|
|
9
|
Ma X, Liu Y, Wang Q, Chen Y, Liu M, Li X,
Xiang R, Wei Y, Duan Y and Han J: Tamoxifen induces the development
of hernia in mice by activating MMP-2 and MMP-13 expression.
Biochim Biophys Acta. 1852.1038–1048. 2015.
|
|
10
|
Nagase H, Visse R and Murphy G: Structure
and function of matrix metalloproteinases and TIMPs. Cardiovasc
Res. 69:562–573. 2006. View Article : Google Scholar : PubMed/NCBI
|
|
11
|
Han KY, Dugas-Ford J, Seiki M, Chang JH
and Azar DT: Evidence for the involvement of MMP14 in MMP2
processing and recruitment in exosomes of corneal fibroblasts.
Invest Ophthalmol Vis Sci. 56:5323–5329. 2015.
|
|
12
|
Siefert SA and Sarkar R: Matrix
metalloproteinases in vascular physiology and disease. Vascular.
20:210–216. 2012. View Article : Google Scholar : PubMed/NCBI
|
|
13
|
Klein T and Bischoff R: Active
metalloproteases of the A disintegrin and metalloprotease (ADAM)
family: Biological function and structure. J Proteome Res.
10:17–33. 2011. View Article : Google Scholar
|
|
14
|
Ishida Y, Kuninaka Y, Nosaka M, Kimura A,
Kawaguchi T, Hama M, Sakamoto S, Shinozaki K, Eisenmenger W and
Kondo T: Immunohistochemical analysis on MMP-2 and MMP-9 for wound
age determination. Int J Legal Med. 129:1043–1048. 2015. View Article : Google Scholar : PubMed/NCBI
|
|
15
|
Tanriverdi-Akhisaroglu S, Menderes A and
Oktay G: Matrix metalloproteinase-2 and -9 activities in human
keloids, hyper-trophic and atrophic scars: A pilot study. Cell
Biochem Funct. 27:81–87. 2009. View
Article : Google Scholar : PubMed/NCBI
|
|
16
|
Gill SE and Parks WC: Metalloproteinases
and their inhibitors: Regulators of wound healing. Int J Biochem
Cell Biol. 40:1334–1347. 2008. View Article : Google Scholar
|
|
17
|
Schultz GS and Wysocki A: Interactions
between extracellular matrix and growth factors in wound healing.
Wound Repair Regen. 17:153–162. 2009. View Article : Google Scholar : PubMed/NCBI
|
|
18
|
Seah CC, Phillips TJ, Howard CE, Panova
IP, Hayes CM, Asandra AS and Park HY: Chronic wound fluid
suppresses proliferation of dermal fibroblasts through a
Ras-mediated signaling pathway. J Invest Dermatol. 124:466–474.
2005. View Article : Google Scholar : PubMed/NCBI
|
|
19
|
Chu X, Wang H, Jiang YM, Zhang YY, Bao YF,
Zhang X, Zhang JP, Guo H, Yang F, Luan YC and Dong YS: Ameliorative
effects of tannic acid on carbon tetrachloride-induced liver
fibrosis in vivo and in vitro. J Pharmacol Sci. 130:15–23. 2016.
View Article : Google Scholar : PubMed/NCBI
|
|
20
|
Takawale A, Zhang P, Patel VB, Wang X,
Oudit G and Kassiri Z: Tissue inhibitor of matrix
metalloproteinase-1 promotes myocardial fibrosis by mediating
CD63-integrin β1 interaction. Hypertension. 69:1092–1103. 2017.
View Article : Google Scholar : PubMed/NCBI
|
|
21
|
Dong J and Ma Q: TIMP1 promotes
multi-walled carbon nanotube-induced lung fibrosis by stimulating
fibroblast activation and proliferation. Nanotoxicology. 11:41–51.
2017. View Article : Google Scholar
|
|
22
|
Chen G, Wang R, Chen H, Wu L, Ge RS and
Wang Y: Gossypol ameliorates liver fibrosis in diabetic rats
induced by high-fat diet and streptozocin. Life Sci. 149:58–64.
2016. View Article : Google Scholar : PubMed/NCBI
|
|
23
|
Livak KJ and Schmittgen TD: Analysis of
relative gene expression data using real-time quantitative PCR and
the 2(−Delta Delta C(T)) method. Methods. 25:402–408. 2001.
View Article : Google Scholar
|
|
24
|
Chapman SJ, Wood B, Drake TM, Young N and
Jayne DG: Systematic review and meta-analysis of prophylactic mesh
during primary stoma formation to prevent parastomal hernia. Dis
Colon Rectum. 60:107–115. 2017. View Article : Google Scholar
|
|
25
|
Funahashi K, Suzuki T, Nagashima Y,
Matsuda S, Koike J, Shiokawa H, Ushigome M, Arai K, Kaneko T,
Kurihara A and Kaneko H: Risk factors for parastomal hernia in
Japanese patients with permanent colostomy. Surg Today.
44:1465–1469. 2014. View Article : Google Scholar :
|
|
26
|
Pilgrim CH, Mcintyre R and Bailey M:
Prospective audit of parastomal hernia: Prevalence and associated
comorbidities. Dis Colon Rectum. 53:71–76. 2010. View Article : Google Scholar
|
|
27
|
Murray BW, Cipher DJ, Pham T and Anthony
T: The impact of surgical site infection on the development of
incisional hernia and small bowel obstruction in colorectal
surgery. Am J Surg. 202:558–560. 2011. View Article : Google Scholar : PubMed/NCBI
|
|
28
|
Höer J, Lawong G, Klinge U and Schumpelick
V: Factors influencing the development of incisional hernia. A
retrospective study of 2,983 laparotomy patients over a period of
10 years. Chirurg. 73:474–480. 2002. View Article : Google Scholar
|
|
29
|
Gurmu A, Matthiessen P, Nilsson S, Påhlman
L, Rutegård J and Gunnarsson U: The inter-observer reliability is
very low at clinical examination of parastomal hernia. Int J
Colorectal Dis. 26:89–95. 2011. View Article : Google Scholar
|
|
30
|
Hotouras A, Murphy J, Power N, Williams NS
and Chan CL: Radiological incidence of parastomal herniation in
cancer patients with permanent colostomy: What is the ideal size of
the surgical aperture? Int J Surg. 11:425–427. 2013. View Article : Google Scholar : PubMed/NCBI
|
|
31
|
Jänes A, Cengiz Y and Israelsson LA:
Preventing parastomal hernia with a prosthetic mesh. Arch Surg.
139:1356–1358. 2004. View Article : Google Scholar : PubMed/NCBI
|
|
32
|
Kanehisa H, Miyatani M, Azuma K, Kuno S
and Fukunaga T: Influences of age and sex on abdominal muscle and
subcutaneous fat thickness. Eur J Appl Physiol. 91:534–537. 2004.
View Article : Google Scholar : PubMed/NCBI
|
|
33
|
Henriksen NA, Yadete DH, Sorensen LT,
Agren MS and Jorgensen LN: Connective tissue alteration in
abdominal wall hernia. Br J Surg. 98:210–219. 2011. View Article : Google Scholar
|
|
34
|
Brown SR, Melman L, Jenkins E, Deeken C,
Frisella MM, Brunt LM, Eagon JC and Matthews BD: Collagen type
I:III ratio of the gastroesophageal junction in patients with
paraesophageal hernias. Surg Endosc. 25:1390–1394. 2011. View Article : Google Scholar
|
|
35
|
Shoulders MD and Raines RT: Collagen
structure and stability. Annu Rev Biochem. 78:929–958. 2009.
View Article : Google Scholar : PubMed/NCBI
|
|
36
|
Henriksen NA, Mortensen JH, Lorentzen L,
Ågren MS, Bay-Jensen AC, Jorgensen LN and Karsdal MA: Abdominal
wall hernias-A local manifestation of systemically impaired quality
of the extracellular matrix. Surgery. 160:220–227. 2016. View Article : Google Scholar : PubMed/NCBI
|
|
37
|
Basson MD: Invited research review:
Cell-matrix interactions in the gut epithelium. Surgery.
133:263–267. 2003. View Article : Google Scholar : PubMed/NCBI
|
|
38
|
Jabłońska-Trypuć A, Matejczyk M and
Rosochacki S: Matrix metalloproteinases (MMPs), the main
extracellular matrix (ECM) enzymes in collagen degradation, as a
target for anticancer drugs. J Enzyme Inhib Med Chem. 31(Suppl 1):
pp. S177–S183. 2016, View Article : Google Scholar
|
|
39
|
Su Y, Wan D and Song W: Dryofragin
inhibits the migration and invasion of human osteosarcoma U2OS
cells by suppressing MMP-2/9 and elevating TIMP-1/2 through
PI3K/AKT and p38 MAPK signaling pathways. Anticancer Drugs.
27:660–668. 2016. View Article : Google Scholar : PubMed/NCBI
|
|
40
|
Agren MS, Jorgensen LN, Andersen M,
Viljanto J and Gottrup F: Matrix metalloproteinase 9 level predicts
optimal collagen deposition during early wound repair in humans. Br
J Surg. 85:68–71. 1998. View Article : Google Scholar : PubMed/NCBI
|
|
41
|
Bigg HF, Rowan AD, Barker MD and Cawston
TE: Activity of matrix metalloproteinase-9 against native collagen
types I and III. FEBS J. 274:1246–1255. 2007. View Article : Google Scholar : PubMed/NCBI
|
|
42
|
Van Doren SR: Matrix metalloproteinase
interactions with collagen and elastin. Matrix Biol. 44-46:224–231.
2015. View Article : Google Scholar : PubMed/NCBI
|
