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J Invest Dermatol. 2003 Jan;120(1):128-34.
Possible involvement of gelatinases in basement membrane damage and wrinkle formation in chronically ultraviolet B-exposed hairless mouse.

Inomata S, Matsunaga Y, Amano S, Takada K, Kobayashi K, Tsunenaga M, Nishiyama T, Kohno Y, Fukuda M.

Skincare Ingredient Research Laboratories, Shiseido Material Development Research Center, 2-2-1 Hayabuchi, Tsuzuki-ku, Yokohama 224-8558, Japan. shinji.inomato.shiseido.co.jp

A number of studies indicate that matrix metalloproteinase might be involved in photoaging, but little is known about their direct contribution to ultraviolet-induced histologic and morphologic changes in the skin in vivo. This study reports the relationship between changes of matrix metalloproteinase activities and ultraviolet B-induced skin changes in hairless mouse. The role of matrix metalloproteinase in the skin changes was studied by topical application of a specific matrix metalloproteinase inhibitor. The backs of mice were exposed to ultraviolet B three times a week for 10 wk. Histologic studies showed that the basement membrane structure was damaged, with epidermal hyperplasia, in the first 2 wk of ultraviolet B irradiation, followed by the appearance of wrinkles, which gradually extended in the latter half of the ultraviolet B irradiation period. We observed enhancement of type IV collagen degradation activity, but not collagenase or matrix metalloproteinase-3 activity, in extracts of ultraviolet B-irradiated, wrinkle-bearing skin. Gelatin zymographic analysis revealed that gelatinases, matrix metalloproteinase-9 and matrix metalloproteinase-2, were significantly increased in the extract. In situ zymographic study clarified that the activity was specifically localized in whole epidermis of ultraviolet B-irradiated, wrinkled skin in comparison with normal skin. The activity was induced around the basal layer of the epidermis by a single ultraviolet exposure of at least one minimal erythema dose. Furthermore, topical application of a specific matrix metalloproteinase inhibitor, CGS27023A, inhibited ultraviolet B-induced gelatinase activity in the epidermis, and its repeated application prevented ultraviolet B-induced damage to the basement membrane, as well as epidermal hyperplasia and dermal collagen degradation. Ultraviolet B-induced wrinkles were also prevented by administration of the inhibitor. These results, taken together, suggest that ultraviolet B-induced enhancement of gelatinase activity in the skin contributes to wrinkle formation through the destruction of basement membrane structure and dermal collagen in chronically ultraviolet B-exposed hairless mouse, and thus topical application of matrix metalloproteinase inhibitors may be an effective way to prevent ultraviolet B-induced wrinkle formation.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=12535209&dopt=Abstract

Mikrobiol Z. 2002 Jul-Aug;64(4):3-11.
[Effect of coordinational germanium compounds on enzyme synthesis and activity]

[Article in Russian]

Seifullina II, Martsinko EE, Batrakova OA, Borzova NV, Ivanko EV, Varbanets LD.

Odessa National University, 2 Dvoryanskaya St., Odessa, 65029, Ukraine.

Germanium complexes (IV) with succinic (H2Suc), oxyethyliminodiacetic (H2Oeida) and iminodisuccinic (H4Ids) acids as well as homo- and heteroligand germanium complexes (IV)--products of interaction of triammonium salt of oxyethylidendiphosphonic acid ((NH4)3HL) and oxyacids: tartaric (H4Tart), citric (H4Citr), trioxyglutaric (H4Toglut) acids have been synthesized. Composition of the obtained complexes: [Ge(OH)2(NaSuc)2].2H2O (I); [Ge(OH) (Oeida).H2O].H2O (II); [Ge(OH)2(NaHIds)2] (III); [Ge(OH)2(NH4)3HL) (H2Tart)] (IV); [Ge(OH)2(NH4)3HL) (H2Citr)] (V); [Ge(OH)2(NH4)3HL) (H2Toglut)] (VI); [Ge(OH)2((NH4)2HL)2] (VII); [Ge (OH)2((NH4)2HL)2] (VII); [Ge(OH)2 (H2O)2(NH4) HL] (VIII) has been determined. The capability of the synthesized compounds has been studied to affect synthesis and activity of the following enzymes: collagenase, alpha-N-acetylgalactosaminidase (alpha-GalNAc-ase) and alpha-galactosidase (alpha-Gal-ase). It has been established that the complexes II-VIII activate biosynthesis of alpha-Gal-ase and alpha-GalNAc-ase, while germanium dioxide (IX) and complex I possess considerable inhibiting effect on synthesis of the above enzymes. It has been also established that all the compounds except for IV increased the activity of both alpha-Gal-ase and alpha-GalNAc-ase. All the considered complexes demonstrated similar reaction with respect to collagenase: they inhibited both synthesis and activity.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=12436865&dopt=Abstract

J Clin Periodontol. 2000 Nov;27(11):832-8.
Acoustic energy affects human gingival fibroblast proliferation but leaves protein production unchanged.

Jones H, Feth L, Rumpf D, Hefti A, Mariotti A.

Section of Periodontology, College of Dentistry, The Ohio State University, 43218-2357, USA.

BACKGROUND, AIMS: Sonic toothbrushes are well-established in oral home care for plaque removal; however, the effects of low frequency acoustic (sonic) energy released from sonic toothbrushes to the cells of the periodontium have not been investigated. The purpose of this study was to evaluate the effects of sonic energy on human gingival fibroblast proliferation and protein production in cell culture. METHODS: Direct and indirect transfer calibration studies found the fundamental frequency of the Sonicare sonic toothbrush to be 261 hertz (Hz) with amplitudes ranging from 70 to 104 decibels (dB) in the human periodontium. Using an in vitro delivery system, which coupled a signal-wave generator with a bone transducer to mimic the energy delivered by the Sonicare toothbrush, the effects of signal, amplitude and duration were evaluated longitudinally using a gingival fibroblast cell culture model. 8 strains of fibroblasts isolated from healthy human gingiva were seeded at 30,000 cells/35 mm culture dish in minimum essential medium supplemented with 10% fetal bovine serum. To ascertain the relationship of the amplitude and the duration of sonic stimulation to cellular proliferation, gingival fibroblasts were subjected 2x daily to 261 Hz sound at various amplitudes (67-97 dB) for 0, 15, 30, 60, and 120 s on days 1, 3, 5, 7, and 10. RESULTS: It was found that either 30 or 120 s of sound exposure for 10 days of treatment had significant effects on cell proliferation in comparison to control cultures. Specifically, at day 10, 87 dB at 261 Hz for 30 s 2x daily resulted in a 25.5% increase in cell number (p<0.001), whereas 87 dB at 261 Hz for 120 s twice daily caused a 30.9% decrease in cell number (p<0.001) when compared to control cultures. When cells are stimulated under optimum acoustic conditions for 10 days, there was no difference between the treatment and control groups for collagen (p=0.897) or noncollagen (p=0.697) protein production. CONCLUSIONS: Sonic energy has been shown to both increase and decrease cellular proliferation depending on exposure time; however, during optimum sound-induced conditions for cellular proliferation, sonic energy had no effect on fibroblast protein production. These data suggest that sonic energy can affect the behavior of cells in culture. Further research into the mechanisms of these changes will provide important information for manipulating cellular behavior.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=11073326&dopt=Abstract

Am J Pathol. 2000 Nov;157(5):1649-59.
Integrin alpha1beta1 and transforming growth factor-beta1 play distinct roles in alport glomerular pathogenesis and serve as dual targets for metabolic therapy.

Cosgrove D, Rodgers K, Meehan D, Miller C, Bovard K, Gilroy A, Gardner H, Kotelianski V, Gotwals P, Amatucci A, Kalluri R.

Department of Genetics, Boys Town National Research Hospital, Omaha, Nebraska, USA. cosgrovoystown.org

Alport syndrome is a genetic disorder resulting from mutations in type IV collagen genes. The defect results in pathological changes in kidney glomerular and inner-ear basement membranes. In the kidney, progressive glomerulonephritis culminates in tubulointerstitial fibrosis and death. Using gene knockout-mouse models, we demonstrate that two different pathways, one mediated by transforming growth factor (TGF)-beta1 and the other by integrin alpha1beta1, affect Alport glomerular pathogenesis in distinct ways. In Alport mice that are also null for integrin alpha1 expression, expansion of the mesangial matrix and podocyte foot process effacement are attenuated. The novel observation of nonnative laminin isoforms (laminin-2 and/or laminin-4) accumulating in the glomerular basement membrane of Alport mice is markedly reduced in the double knockouts. The second pathway, mediated by TGF-beta1, was blocked using a soluble fusion protein comprising the extracellular domain of the TGF-beta1 type II receptor. This inhibitor prevents focal thickening of the glomerular basement membrane, but does not prevent effacement of the podocyte foot processes. If both integrin alpha1beta1 and TGF-beta1 pathways are functionally inhibited, glomerular foot process and glomerular basement membrane morphology are primarily restored and renal function is markedly improved. These data suggest that integrin alpha1beta1 and TGF-beta1 may provide useful targets for a dual therapy aimed at slowing disease progression in Alport glomerulonephritis.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=11073824&dopt=Abstract

Arterioscler Thromb Vasc Biol. 2000 Nov;20(11):E113-9.
Coimmobilized native macromolecular heparin proteoglycans strongly inhibit platelet-collagen interactions in flowing blood.

Kauhanen P, Kovanen PT, Lassila R.

Wihuri Research Institute, Helsinki, Finland.

We coimmobilized mast cell-derived heparin proteoglycans (HEP-PGs) of very high molecular weight (750 kDa) or unfractionated heparin (UFH) on coverslips together with collagen without altering the amount of immobilized collagen. Subsequently, platelet-collagen interactions were studied under both flowing and static conditions in D-phenylalanyl-L-prolyl-L-arginine chloromethyl ketone-anticoagulated blood and platelet-rich plasma (PRP), respectively. At a high shear rate (1600 1/s), the mean platelet deposition (PD) on collagen monomers was 7.5+/-6.1x10(6)/cm(2) (n=5). When the monomers were coimmobilized with UFH, PD was inhibited by 73% (2.0+/-1.2x10(6)/cm(2)), whereas HEP-PG completely blocked it (0. 42+/-0.38x10(6)/cm(2); P<0.05). Also, when collagen fibrils were used for coating, HEP-PG significantly inhibited PD. At a low shear rate (200 1/s) and under static conditions in PRP, the inhibitory effect of HEP-PG on PD was less marked. Inhibition of glycoprotein IIb/IIIa did not affect PD on coimmobilized HEP-PG in contrast to coimmobilized UFH or collagen alone. As a sign of inactivation, platelets adhering to the HEP-PG surface released considerably less beta-thromboglobulin than did those adhering to pure collagen. In summary, immobilized HEP-PG strongly inhibited PD on collagen by attenuating adhesion-induced platelet activation. The stronger effect on collagen monomers suggests the inhibition of glycoprotein Ia/IIa-mediated activation.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=11073864&dopt=Abstract

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