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Toxicol Lett. 2000 Sep 30;117(1-2):11-23.
Interactions between benzo[a]pyrene and UVA light affecting ATP levels, cytoskeletal organization, and resistance to trypsinization.

Seagrave JC, Burchiel SW.

Lovelace Respiratory Research Institute, The University of New Mexico College of Pharmacy Toxicology Program, Albuquerque, NM 87131-1341, USA.

Polycyclic aromatic hydrocarbons affect cells in many ways, including covalent modifications of DNA, participation in redox cycling, and alterations in cellular signaling pathways. Similarly, exposure to ultraviolet (UV) light may modify DNA, generate reactive oxygen species, and alter signaling. Because environmental conditions may interact to affect cellular functions, we investigated the combined effects of benzo[a]pyrene (BaP) and UV light in a cell line in which BaP-induced alterations in Ca(2+) homeostasis have previously been shown. Exposure of MCF-10A cells to BaP (18 h) followed by a brief (5 min) exposure to UVA resulted in resistance to trypsinization of cells grown on type I collagen (Vitrogen). This effect was not seen following treatment with BaP or UVA alone nor with benzo(e)pyrene (BeP)+UVA. BaP+UVA light also caused actin filaments to reorganize from typical stress fibers to substrate-associated aggregates of actin and caused depletion of cellular adenosine triphosphate (ATP). The effects of BaP+UVA on adhesion and actin aggregate formation were partially prevented by treatment with reduced glutathione. Depletion of cellular ATP affected resistance to trypsinization and actin organization in a similar manner. Thus, these studies suggest a redox-sensitive interaction between BaP+UVA light to deplete cellular ATP levels, resulting in resistance to trypsinization and actin filament reorganization in MCF-10A cells.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=11033229&dopt=Abstract

Bone. 2000 Oct;27(4):535-40.
Effects of spaceflight and simulated weightlessness on longitudinal bone growth.

Sibonga JD, Zhang M, Evans GL, Westerlind KC, Cavolina JM, Morey-Holton E, Turner RT.

Department of Orthopedics, Mayo Clinic, Rochester, MN 55905, USA. sibonga.jeaayo.edu

Indirect measurements have suggested that spaceflight impairs bone elongation in rats. To test this possibility, our laboratory measured, by the fluorochrome labeling technique, bone elongation that occurred during a spaceflight experiment. The longitudinal growth rate (LGR) in the tibia of rats in spaceflight experiments (Physiological Space Experiments 1, 3, and 4 and Physiological-Anatomical Rodent Experiment 3) and in two models of skeletal unloading (hind-limb elevation and unilateral sciatic neurotomy) were calculated. The effects of an 11 day spaceflight on gene expression of cartilage matrix proteins in rat growth plates were also determined by northern analysis and are reported for the first time in this study. Measurements of longitudinal growth indicate that skeletal unloading generally did not affect LGR, regardless of age, strain, gender, duration of unloading, or method of unloading. There was, however, one exception with 34% suppression in LGR detected in slow-growing, ovariectomized rats skeletally unloaded for 8 days by hind-limb elevation. This detection of reduced LGR by hind-limb elevation is consistent with changes in steady-state mRNA levels for type II collagen (-33%) and for aggrecan (-53%) that were detected in rats unloaded by an 11 day spaceflight. The changes detected in gene expression raise concern that spaceflight may result in changes in the composition of extracellular matrix, which could have a negative impact on conversion of growth-plate cartilage into normal cancellous bone by endochondral ossification.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=11033449&dopt=Abstract

Bone. 2000 Oct;27(4):551-7.
Expression of extracellular matrix genes: transforming growth factor (TGF)-beta1 and ras in tibial fracture healing of lathyritic rats.

Ekholm EC, Ravanti L, Kahari V, Paavolainen P, Penttinen RP.

Department of Medical Biochemistry and Medicity Research Laboratory, University of Turku, Turku, Finland.

Experimental osteolathyrism, induced by dietary aminoacetonitrile (AAN), was used to study the effect of altered extracellular matrix on the expression of connective tissue components in long bone healing. AAN inhibits lysyl oxidase, which is needed for the formation of collagen cross-link precursors, and is also shown to act as a regulator of Ras. Fractured tibias in lathyritic rats develop excessive amounts of mechanically weak callus tissue with irregular cartilage and reduced glycosaminoglycan accumulation. Cartilage-specific proteins (collagen types II, IX, and X and aggrecan) were expressed temporally much wider in lathyritic calluses than in the controls, and active transcription was observed even during the fibrous and ossifying stages. Soft connective tissue was still present in 2- and 3-week-old lathyritic calluses and could explain the elevated type III collagen, biglycan, and decorin mRNA levels. Both transforming growth factor (TGF)-beta1 and c-Ha-ras, which control cell growth and differentiation, were upregulated during the cartilaginous stage. The maximal expression of TGF-beta1 preceded that of ras in osteolathyrism.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=11033451&dopt=Abstract

J Biomed Mater Res. 2000 Dec 15;52(4):716-24.
Beta-1 integrin expression by human nasal chondrocytes in microcarrier spinner culture.

Bouchet BY, Colon M, Polotsky A, Shikani AH, Hungerford DS, Frondoza CG.

Johns Hopkins University, Department of Orthopaedic Surgery, Division of Arthritis Surgery, Good Samaritan Hospital, Professional Office Building, G-1, 5601 Loch Raven Boulevard, Baltimore, Maryland 21239, USA.

Beta-1 integrin plays a major role in cell attachment and is believed to be involved in mediating the interactions of chondrocytes with their environment. We previously reported that articular chondrocytes propagated in microcarrier spinner culture proliferated and reexpressed their chondrocytic protein. The goal of the present study was to investigate the expression of beta-1 integrin by chondrocytes growing on the surface of microcarriers. Nasal chondrocytes (4 x 10(3)/cm(2)) were seeded on microcarriers and incubated at 37 degrees C, 5% CO(2), 60 rpm. Expression of chondrocyte markers and beta-1 integrin was determined using reverse transcriptase-polymerase chain reaction and immunocytochemical analyses. De novo synthesis of sulfate-containing proteoglycans was studied using 35SO(4) incorporation techniques. Like articular chondrocytes propagated in microcarrier spinner culture, nasal chondrocytes expressed high levels of collagen type II mRNA, whereas collagen type I mRNA levels were low. Aggrecan mRNA was detectable and levels of de novo 35SO(4) incorporation were high. Chondrocytes immunostained intensely for collagen type II and keratan sulfate but did not stain for collagen type I. beta-1 integrin mRNA levels were high, and the protein was immunolocalized to regions of cell-to-cell or cell-to-microcarrier contact. The fact the chondrocytes expressed high levels of beta-1 integrin raises the possibility that this integrin molecule has a role in the maintenance of the chondrocytic phenotype. 2000 John Wiley & Sons, Inc.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=11033555&dopt=Abstract

J Biomed Mater Res. 2000 Dec 15;52(4):725-37.
Integrin-mediated signaling regulates AP-1 transcription factors and proliferation in osteoblasts.

Cowles EA, Brailey LL, Gronowicz GA.

Department of Orthopaedics, MC-1110, University of Connecticut Health Center, Farmington, Connecticut 06032, USA.

Since osteoblast proliferation is critical for bone development, the effect of bone extracellular matrix (ECM) proteins on osteoblast signaling and proliferation in serum-free medium was investigated. Proliferation was highest in primary rat calvarial osteoblasts cells grown on fibronectin but less on type I collagen; osteonectin and poly-L-lysine did not support early proliferation. Fibronectin and type I collagen binding requires integrins, whereas cell adhesion to osteonectin or poly-L-lysine does not involve integrins. Therefore, the role of integrins in osteoblast signaling, leading to the induction of AP-1 transcription factors (c-fos and c-jun) which are important in cell proliferation, was studied. c-fos and c-jun message levels were increased at 60 min in osteoblasts plated onto fibronectin or collagen, but not in cells on osteonectin or poly-L-lysine. Protein synthesis was not required for c-fos mRNA expression; however, kinase activity was necessary for c-fos induction. In cells plated onto fibronectin, c-fos mRNA levels were controlled by protein kinase C and phosphotyrosine kinase signaling pathways. In contrast, c-fos levels in collagen-adhering cells may involve protein kinase A. The signaling pathway involving the phosphorylation of focal adhesion kinase and mitogen-activated kinases was also shown to be transiently increased in osteoblasts on fibronectin and type I collagen, but not in cells on poly-L-lysine. These results demonstrate that osteoblast binding to the extracellular matrix through integrins induces c-fos and c-jun, and that both fibronectin and collagen affect these AP-1 transcription factors through protein kinase-sensitive pathways. Thus, osteoblast proliferation is modulated differentially by specific ECM components. 2000 John Wiley & Sons, Inc.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=11033556&dopt=Abstract

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