Selective processing of a follicular matrix metalloproteinase-2 isoform by human oviducal fluid

The present study demonstrates that a unique isoform of matrix metalloproteinase (MMP)-2 present in human follicular fluid (FF) can be processed selectively by human oviducal fluid (OF). A gelatin zymogram of untreated FF showed distinct 88-, 84- and 62-kDa gelatinases. Treatment of FF with EDTA resulted in the appearance of 110-kDa gelatinase (GA110). Most gelatinases, except for the 88- and 84-kDa gelatinases, were abolished by pretreatment with EDTA or phenanthroline, but not by pretreatment with a serine/threonine protease inhibitor. When EDTA-pretreated FF was mixed with OF, the GA110 of the FF was specifically reduced. The reduction in GA110 was dependent upon the amount of OF protein and the incubation period after mixing. Treatment of FF with aminophenylmercuric acetate reduced GA110 activity, but this reduction was accompanied by a concomitant increase of 62-kDa gelatinase activity. Anti-human MMP-2 antibody strongly reacted with both GA110 and 62-kDa gelatinases of FF, but only GA110 immunoreactivity was abolished when FF was mixed with OF. The results suggest that the GA110 of FF is an MMP-2 isoform that can be processed selectively by OF.

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Matrix metalloproteinase 2 level in human follicular fluid is a reliable marker of human oocyte maturation in in vitro fertilization and intracytoplasmic sperm injection cycles

Reproductive Biology and Endocrinology ◽

10.1186/s12958-015-0099-8 ◽

2015 ◽

Vol 13 (1) ◽

Cited By ~ 5

Author(s):

Wen-Jui Yang ◽

Fon-Chang Liu ◽

Jih-Sheng Hsieh ◽

Ching-Hung Chen ◽

Shun-Yu Hsiao ◽

...

Keyword(s):

In Vitro Fertilization ◽

Matrix Metalloproteinase ◽

Oocyte Maturation ◽

Follicular Fluid ◽

Matrix Metalloproteinase 2 ◽

Human Oocyte ◽

Human Follicular Fluid ◽

Vitro Fertilization ◽

Reliable Marker

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Protease Inhibitor-Dependent Inhibition of Light-Induced Stomatal Opening

Frontiers in Plant Science ◽

10.3389/fpls.2021.735328 ◽

2021 ◽

Vol 12 ◽

Author(s):

Tenghua Wang ◽

Wenxiu Ye ◽

Yin Wang ◽

Maoxing Zhang ◽

Yusuke Aihara ◽

...

Keyword(s):

Matrix Metalloproteinase ◽

Protease Inhibitor ◽

Signaling Pathway ◽

Stomatal Closure ◽

Screening Method ◽

Stomatal Opening ◽

Matrix Metalloproteinase 2 ◽

Aba Signaling ◽

Bioinformatics Analyses ◽

Chemical Screening

Stomata in the epidermis of plants play essential roles in the regulation of photosynthesis and transpiration. Stomata open in response to blue light (BL) by phosphorylation-dependent activation of the plasma membrane (PM) H+-ATPase in guard cells. Under water stress, the plant hormone abscisic acid (ABA) promotes stomatal closure via the ABA-signaling pathway to reduce water loss. We established a chemical screening method to identify compounds that affect stomatal movements in Commelina benghalensis. We performed chemical screening using a protease inhibitor (PI) library of 130 inhibitors to identify inhibitors of stomatal movement. We discovered 17 PIs that inhibited light-induced stomatal opening by more than 50%. Further analysis of the top three inhibitors (PI1, PI2, and PI3; inhibitors of ubiquitin-specific protease 1, membrane type-1 matrix metalloproteinase, and matrix metalloproteinase-2, respectively) revealed that these inhibitors suppressed BL-induced phosphorylation of the PM H+-ATPase but had no effect on the activity of phototropins or ABA-dependent responses. The results suggest that these PIs suppress BL-induced stomatal opening at least in part by inhibiting PM H+-ATPase activity but not the ABA-signaling pathway. The targets of PI1, PI2, and PI3 were predicted by bioinformatics analyses, which provided insight into factors involved in BL-induced stomatal opening.

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The expression of matrix metalloproteinase-9 in human follicular fluid is associated with in vitro fertilisation pregnancy

BJOG An International Journal of Obstetrics & Gynaecology ◽

10.1111/j.1471-0528.2005.00574.x ◽

2005 ◽

Vol 112 (7) ◽

pp. 946-951 ◽

Cited By ~ 19

Author(s):

Dong-Mok Lee ◽

Tae-Kyun Lee ◽

Hai-Bum Song ◽

Cheorl-Ho Kim

Keyword(s):

Matrix Metalloproteinase ◽

Follicular Fluid ◽

Matrix Metalloproteinase 9 ◽

In Vitro Fertilisation ◽

Human Follicular Fluid ◽

Metalloproteinase 9

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Bovine Follicular Fluid and Serum Share a Unique Isoform of Matrix Metalloproteinase-2 That Is Degraded by the Oviductal Fluid1

Biology of Reproduction ◽

10.1095/biolreprod65.6.1726 ◽

2001 ◽

Vol 65 (6) ◽

pp. 1726-1731 ◽

Cited By ~ 8

Author(s):

Minjung Kim ◽

Minjeong Hong ◽

Jisoo Kim ◽

Haekwon Kim ◽

Seung-Jae Lee ◽

...

Keyword(s):

Matrix Metalloproteinase ◽

Follicular Fluid ◽

Matrix Metalloproteinase 2

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Matrix metalloproteinase-2 activity, protein, mRNA, and tissue inhibitors in small arteries from pregnant and relaxin-treated nonpregnant rats

Journal of Applied Physiology ◽

10.1152/japplphysiol.01330.2005 ◽

2006 ◽

Vol 100 (6) ◽

pp. 1955-1963 ◽

Cited By ~ 44

Author(s):

Arundhathi Jeyabalan ◽

Laurie J. Kerchner ◽

Michelle C. Fisher ◽

Jonathan T. McGuane ◽

Ketah D. Doty ◽

...

Keyword(s):

Matrix Metalloproteinase ◽

Gelatin Zymography ◽

Renal Arteries ◽

Mesenteric Arteries ◽

Tissue Inhibitor Of Metalloproteinase ◽

Matrix Metalloproteinase 2 ◽

Pregnant Rats ◽

Gelatinase Activity ◽

Small Arteries ◽

Major Factors

Vascular gelatinase activity is essential for pregnancy- and relaxin (Rlx)-induced renal vasodilation and hyperfiltration in rats. The objective of this study was to further elucidate the mechanisms for the increase in vascular matrix metalloproteinase (MMP)-2 activity caused by pregnancy and Rlx. We first corroborated our earlier work by showing that pro- and active forms of MMP-2 were increased in small renal arteries from pregnant compared with virgin rats and Rlx-treated compared with vehicle-treated nonpregnant rats. We next investigated other artery types and showed that MMP-2 activity was upregulated in mesenteric arteries from pregnant rats (pro-MMP-2 by 50% and active MMP-2 by 40%, both P < 0.05) and from Rlx-treated nonpregnant rats (pro-MMP-2 by 50% and active MMP-2 by 90%, both P < 0.005) compared with their respective controls. To corroborate these results obtained by gelatin zymography, pro-MMP-2 protein was determined by Western analysis in the same small arteries. Pro-MMP-2 protein was increased in small renal arteries from pregnant compared with virgin rats and from Rlx- compared with vehicle-treated nonpregnant rats: pro-MMP-2-to-β-actin ratio = 0.29 vs. 0.21 ( P < 0.01) and 0.43 vs. 0.32 ( P < 0.005). Findings were similar for mesenteric arteries. MMP-2 mRNA as measured by real-time PCR was increased in small renal arteries from pregnant and Rlx-treated nonpregnant rats compared with their respective controls. There were no significant differences in tissue inhibitor of metalloproteinase (TIMP-1 or TIMP-2) activity by reverse zymography in small renal arteries. Thus increases in MMP-2 mRNA and protein expression are major factors contributing to increased MMP-2 activity in small arteries from pregnant and Rlx-treated nonpregnant rats.

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