The Effect of Compression and Lying Down on Local Matrix Metalloproteinases From the Dependent Leg in Healthy Subjects and Varicose Vein Patients

2018 ◽  
Vol 6 (2) ◽  
pp. 296-297
Author(s):  
Christopher R. Lattimer ◽  
Daniela Ligi ◽  
Ferdinando Mannello ◽  
Evi Kalodiki

2000 ◽  
Vol 15 (2) ◽  
pp. 64-70 ◽  
Author(s):  
J. Buján ◽  
F. Jurado ◽  
M. J. Gimeno ◽  
N. García-Honduvilla ◽  
G. Pascual ◽  
...  

Objective: An evaluation of the proteoglycan perlecan, collagen I and III, and metalloproteinases MMP−1, −2, −3 and −9 was performed to explore the possible relationships between ageing, affected vein region and reactive state of the varicose vein wall. Methods: Segments of saphenous vein were obtained from healthy subjects and from those with varicose veins. The vein specimens were subdivided according to subject age (<50/^50) and vein source (distal/proximal). Results: The walls of control vein specimens acquired a more collagenous appearance with age. These changes were not accompanied by significant modifications in the immunohistochemical markers used. In specimens from young patients, proximal varicose vein segments showed an increase in MMP-1, MMP-2 and MMP-9 expression. Subjects of more advanced age showed an increase in perlecan expression. Conclusion: This increase in MMPs could lead to the acceleration of the final fibrosclerotic process characteristic of the varicose vein wall.



2014 ◽  
Vol 2014 ◽  
pp. 1-10 ◽  
Author(s):  
Veronica Tisato ◽  
Giorgio Zauli ◽  
Sergio Gianesini ◽  
Erica Menegatti ◽  
Laura Brunelli ◽  
...  

The expression of proinflammatory cytokines/chemokines has been reported inin vitro/ex vivosettings of chronic venous insufficiency (CVI), but the identification of circulating mediators that might be associated with altered hemodynamic forces or might represent innovative biomarkers is still missing. In this study, the circulating levels of 31 cytokines/chemokines involved in inflammatory/angiogenic processes were analysed in (i) CVI patients at baseline before surgical hemody namic correction, (ii) healthy subjects, and (iii) CVI patients after surgery. In a subgroup of CVI patients, in whom the baseline levels of cytokines/chemokines were analyzed in paired blood samples obtained from varicose vein and forearm vein, EGF, PDGF, and RANTES were increased at the varicose vein site as compared to the general circulation. Moreover, while at baseline, CVI patients showed increased levels of 14 cytokines/chemokines as compared to healthy subjects, 6 months after surgery, 11 cytokines/chemokines levels were significantly reduced in the treated CVI patients as compared to the CVI patients before surgery. Of note, a patient who exhibited recurrence of the disease 6 months after surgery, showed higher levels of EGF, PDGF, and RANTES compared to nonrecurrent patients, highlighting the potential role of the EGF/PDGF/RANTES triad as sensitive biomarkers in the context of CVI.



2019 ◽  
Vol In Press (In Press) ◽  
Author(s):  
Zohreh Dalirsani ◽  
Atessa Pakfetrat ◽  
Zahra Delavarian ◽  
Seyed Isaac Hashemy ◽  
Leila Vazifeh Mostaan ◽  
...  


2021 ◽  
Vol 74 (1-2) ◽  
pp. 50-56
Author(s):  
Arzu Sanli ◽  
Musa Ozturk ◽  
Aysun Soysal ◽  
Yasemin Doventas ◽  
Fulya Basoglu ◽  
...  

Matrix metalloproteinases (MMPs), which are synthesized by many cell groups and responsible for the destruction of matrix proteins, and endogen tissue inhibitors of MMPs (TIMPs) have a role in the pathogenesis of Multiple Sclerosis (MS) by affecting the blood-brain barrier. We aimed to investigate the role of MMPs and TIMPs in the immunopathogenesis and in the course of multiple sclerosis (MS). We enrolled 25 relapsing remitting MS patients, who had a definite MS diagnosis according to McDonald criteria and 25 healthy subjects similar for age and gender as control group. MMP-9- and TIMP-1 levels were measured twice in patient group (one time during an attack and one in remission) and once in healthy subjects. MMP-9- and TIMP-levels of patients during attack and remission period and MMP-9/TIMP-1 ratio were found significantly higher than in the control subjects. In patient group MMP-9 and TIMP-1 levels and MMP-9/TIMP-1 ratio during attacks were not significantly different than during remission period. However, when subdivided according to their number of attacks, patients with 2 attacks had significantly higher levels during attack period comparing to remission period (p<0.05); in case of patients with more than 2 attacks did not have a statistically significant difference in attack and remission periods. Matrix metalloproteinases are important actors in MS immunopathogenesis, particularly in the early period and inhibitor agents for these enzymes can be used as a treatment option.





1994 ◽  
Vol 73 (8) ◽  
pp. 1397-1406 ◽  
Author(s):  
M. Makela ◽  
T. Salo ◽  
V.-J. Uitto ◽  
H. Larjava

Proteolytic enzymes released by the host cells are associated with the tissue destruction in periodontal diseases. Matrix metalloproteinases (MMPs) have the primary role in this process, since, in concert, they can degrade most of the extracellular matrix components. In the present study, we investigated MMP-2 and MMP-9 in oral fluids of healthy subjects and periodontitis patients and the contributions of different oral cells to the enzyme production. The enzymograms revealed that the main gelatinase in oral rinses, crevicular fluid, and whole saliva migrated at 92 kDa. Activity was also detected at 200 kDa and 130 kDa and minor activity at 86 kDa, 72 kDa, and 40 kDa. Traces of gelatinolytic activity were also detected in pure parotid secretions. The 92-kDa enzyme was identified to MMP-9 and the 200-kDa gelatinase to MMP-2, by means of specific anti-72-kDa antiserum. Gingival keratinocytes produced mainly MMP-9, while gingival and granulation tissue fibroblasts expressed MMP-2. Glandular tissue contained mainly MMP-9, and mRNA for MMP-9 was also found in acinar epithelial cells. Periodontitis patients had significantly higher levels of MMP-9 than healthy subjects. Also, MMP-2 was elevated in periodontitis patients. Periodontal treatment reduced the amount of gelatinases dramatically. This study shows that gelatinases are produced by various cells in the oral cavity. The amount of gelatinases is elevated during periodontal disease, while conventional periodontal treatment efficiently reduces the levels these enzymes. We suggest that MMP-2 and MMP-9 could participate in tissue destruction in periodontitis.



Author(s):  
R. Chen

ABSTRACT:Cutaneous reflexes in the upper limb were elicited by stimulating digital nerves and recorded by averaging rectified EMG from proximal and distal upper limb muscles during voluntary contraction. Distal muscles often showed a triphasic response: an inhibition with onset about 50 ms (Il) followed by a facilitation with onset about 60 ms (E2) followed by another inhibition with onset about 80 ms (12). Proximal muscles generally showed biphasic responses beginning with facilitation or inhibition with onset at about 40 ms. Normal ranges for the amplitude of these components were established from recordings on 22 arms of 11 healthy subjects. An attempt was made to determine the alterent fibers responsible for the various components by varying the stimulus intensity, by causing ischemic block of larger fibers and by estimating the afferent conduction velocities. The central pathways mediating these reflexes were examined by estimating central delays and by studying patients with focal lesions



2003 ◽  
Vol 70 ◽  
pp. 125-133 ◽  
Author(s):  
Tim E. Cawston ◽  
Jenny M. Milner ◽  
Jon B. Catterall ◽  
Andrew D. Rowan

We have investigated proteinases that degrade cartilage collagen. We show that pro-inflammatory cytokines act synergistically with oncastatin M to promote cartilage collagen resorption by the up-regulation and activation of matrix metalloproteinases (MMPs). The precise mechanisms are not known, but involve the up-regulation of c-fos, which binds to MMP promoters at a proximal activator protein-1 (AP-1) site. This markedly up-regulates transcription and leads to higher levels of active MMP proteins.



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