ALBERT — All Library Books, journals and Electronic Records Telegrafenberg

1

Electronic Resource

Species Differences in Growth Requirements for Bone Marrow Stromal Fibroblast Colony Formation In Vitro (1996)

Kuznetsov, S. ; Gehron Robey, P.

Springer

Calcified tissue international 59 (1996), S. 265-270

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ISSN: 1432-0827

Keywords: Key words: Marrow — Stromal — Fibroblast — Colony — Formation.

Source: Springer Online Journal Archives 1860-2000

Topics: Biology , Medicine , Physics

Notes: Abstract. The marrow stromal fibroblast (MSF) population has been shown to include precursor cells for at least five types of connective tissue: bone, cartilage, adipose tissue, fibrous tissue, and hematopoiesis-supporting reticular stroma. In this study, growth requirements for MSF colony formation were studied in vitro. In order to exclude the influence of nonadherent cells, after a period of initial adhesion of bone marrow cells in serum-containing medium nonadherent cells were removed. Further cultivation was carried out in either serum-containing or serum-free conditions, with or without feeder cells (irradiated bone marrow cells). This approach revealed differences between animal species in initial MSF growth requirements. In serum-containing conditions, mouse MSF precursor cells (colony-forming units-fibroblast, CFU-Fs) were shown to be feeder cell dependent: MSF colonies were formed only in the presence of feeder cells. Guinea pig CFU-Fs were partially feeder cell dependent, whereas human CFU-Fs were feeder cell independent. In serum-free conditions, CFU-Fs of all three species were feeder cell dependent. The difference between the growth requirements for mouse and human MSFs was not caused by serum origin or concentration, feeder cell origin, or differences in the preparation of marrow cell suspensions.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1007/s002239900121

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2

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Efficient Gene Transfer into Normal Human Skeletal Cells Using Recombinant Adenovirus and Conjugated Adenovirus-DNA Complexes (1999)

Sommer, B. ; Kuznetsov, S. A. ; Robey, P. G. ; [et al.]

Springer

Calcified tissue international 64 (1999), S. 45-49

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ISSN: 1432-0827

Keywords: Key words: Transfection — Gene transfer — Adenovirus — Polylysine-conjugate — Skeletal cells.

Source: Springer Online Journal Archives 1860-2000

Topics: Biology , Medicine , Physics

Notes: Abstract. In order to assess efficient DNA gene transfer into human primary cell cultures derived from the skeleton we tested two viral-based procedures. First, replication-deficient recombinant adenoviruses (ADV) were used to infect post-confluent human marrow stromal fibroblasts (HMSF) and human trabecular bone (HTB) cells. Both cell types were readily infected by modified adenoviral vectors carrying a reporter gene making this virus an attractive candidate to facilitate DNA gene transfer. In a second approach we coincubated DNA with ADV that had polylysine (PLL) covalently attached. With this ADV/PLL/DNA complex, very efficient gene transfer into multilayered HMSF and HTB cell cultures was observed, and DNA coincubated with unmodified ADV failed to be effectively transferred. These data imply that the covalently bound PLL more effectively binds exogenous DNA, resulting in a highly efficient internalization event in both cell types. Thus, this latter method has many advantages over conventional ADV gene transfer procedures. It is simple, rapid, and it does not require engineering of DNA into the viral genome, thereby allowing transfer of large fragments of DNA.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1007/s002239900577

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3

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The anatomy of bone sialoprotein immunoreactive sites in bone as revealed by combined ultrastructural histochemistry and immunohistochemistry (1995)

Riminucci, M. ; Silvestrini, G. ; Bonucci, E. ; [et al.]

Springer

Calcified tissue international 57 (1995), S. 277-284

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ISSN: 1432-0827

Keywords: Bone sialoprotein ; osteoblast ; Bone matrix ; Electron microscopy ; Immunolocalization ; noncollagenous protein

Source: Springer Online Journal Archives 1860-2000

Topics: Biology , Medicine , Physics

Notes: Abstract Bone sialoprotein was immunolocalized at the EM level in thin Lowicryl K4M sections of rat bone. Because of the unconventional EM morphology of the bone matrix seen in thin demineralized acrylate sections, the pattern of immunolabeling was compared with detailed structural images of demineralized bone obtained using an en bloc treatment of tissue samples with the cationic electron ‘dye’, Malachite Green (MG), which provides stabilization and retention of anionic material throughout specimen processing. A system of structures corresponding to the sites of bone sialoprotein (BSP) immunoreactivity, as seen in Lowicryl K4M thin sections, could be readily identified in the MG-treated, expoxy thin sections. This system includes the cement lines, and aggregates of similar material within mineralized bone and mineralizing osteoid. The virtual identity of BSP distribution with the arrangement of the MG-visualized material indicates that a BSP-enriched, noncollagenous phase can be demonstrated using different, unrelated tissue preparation and imaging protocols for EM. Besides improving our understanding of the distribution of bone sialoprotein in bone, these data assign a previously unrecognized structural dimension to noncollagenous material in the bone matrix.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1007/BF00298883

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4

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The Human Bone Sialoprotein Gene Contains an NF-E1/YY1 Cis-Acting Sequence with Putative Regulatory Activity (1997)

Kerr, J. M. ; Hiscock, D. R. R. ; Grzesik, W. ; [et al.]

Springer

Calcified tissue international 60 (1997), S. 276 -282

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ISSN: 1432-0827

Keywords: Key words: Bone sialoprotein — UMR106-01 BSP — YY1 motif — CCAAT — TATA motif.

Source: Springer Online Journal Archives 1860-2000

Topics: Biology , Medicine , Physics

Notes: Abstract. Bone sialoprotein (BSP) is a noncollagenous matrix glycoprotein localized predominantly in mineralized tissues but also detected in extraskeletal sites undergoing focal mineralization. We have previously characterized the human BSP gene and have shown that the upstream sequence contains inverted TATA and CCAAT motifs at the expected locations from the transcriptional start site (J. M. Kerr et al. [13]) and a potential YY1 binding motif located within the first 30 bp of intron 1 of the human gene. Deletion analyses of the human BSP promoter/exon 1 sequence fused to a CAT reporter gene indicate that CCAAT enhances basal transcription of BSP in transiently transfected rat UMR106-01 BSP osteosarcoma and rat skin fibroblasts. Though this enhancing activity was lost with inclusion of 68 bp of intron containing a YY1 motif in these constructs, reporter activity in the UMR106-01-BSP cells was elevated four- to seven-fold relative to that of rat fibroblasts. Gel electrophoretic mobility shift, UV-crosslinking, and southwestern experiments indicate that YY1 is present only in the extracts of nuclei isolated from the UMR cells and may contribute to the elevated transcriptional activity of the human BSP promoter construct in UMR106-01-BSP.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1007/s002239900229

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5

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Bone marrow interface: Preferential attachment of an osteoblastic marrow stromal cell line (1995)

Benayahu, D. ; Fried, A. ; Efraty, M. ; [et al.]

New York, N.Y. : Wiley-Blackwell

Journal of Cellular Biochemistry 59 (1995), S. 151-160

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ISSN: 0730-2312

Keywords: stromal cells ; osteoblasts ; attachment ; bone matrix ; bone formation ; Life and Medical Sciences ; Cell & Developmental Biology

Source: Wiley InterScience Backfile Collection 1832-2000

Topics: Biology , Chemistry and Pharmacology , Medicine

Notes: In this study, we report on the cell adhesion properties of marrow stromal cells to extracellular matrix components such as collagen and noncollagenous proteins. The osteoblastic cells and their non-osteoblastic counter-parts (MBA series) from the marrow stroma differentially recognized a spectrum of extracellular matrix proteins. The osteoblastic cells, MBA-15, preferentially attached to bone matrix proteins, whereas fibroendothelial MBA-2.1 and adipocytic 14F1.1 cells did not. The MBA-15 cells demonstrated a preference in their attachment to fibronectin 〉 mixture of collagens 〉 bone matrix extracts 〉 collagen type 1 〉 noncollagenous proteins. Clonal subpopulations derived from the MBA-15 cell line representing various stages along the osteogenic lineage expressed differential attachment preference. MBA-15.4, a less differentiated clonal line, was compared to MBA-15.6, a mature cell line. © 1995 Wiley-Liss, Inc.

Additional Material: 3 Ill.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1002/jcb.240590204

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6

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Human bone cell enzyme expression and cellular heterogeneity: Correlation of alkaline phosphatase enzyme activity with cell cycle (1990)

Fedarko, N. S. ; Bianco, P. ; Vetter, U. ; [et al.]

New York, NY [u.a.] : Wiley-Blackwell

Journal of Cellular Physiology 144 (1990), S. 115-121

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ISSN: 0021-9541

Keywords: Life and Medical Sciences ; Cell & Developmental Biology

Source: Wiley InterScience Backfile Collection 1832-2000

Topics: Biology , Medicine

Notes: Alkaline phosphatase, long implicated in biomineralization, is a feature of the osteoblast phenotype. Yet in cultured bone cells, only a fraction stain positive histochemically. To determine whether osteoblast enzyme expression reflects cellular heterogeneity with respect to cell cycle distribution or length of time in culture, the activities of alkaline phosphatase, tartrate-resistant and -sensitive acid phosphatases, and non-specific esterases were assayed kinetically and histo-chemically. In asynchronous subconfluent cultures, 〈 15% of the cells stained positive and assayed activity was 0.04 IU/106 cells/cm2. After 1 week, the percent of alkaline phosphatase positive-staining cells increased 5-fold, while activity increased 10-fold. Non-specific esterases and tartrate-sensitive acid phosphatase were constitutive throughout time in culture, whereas tartrate-resistant acid phos-phatase activity appeared after 2 weeks. Cell cycle analysis of human bone cells revealed a growth fraction of 80%, an S phase of 8.5 h, G2 + 1/2 M of 4 h, and a G1 of 25-30 h. In synchronous cultures induced by a thymidine-aphidicolin protocol, alkaline phosphatase activity dropped precipitously at M phase and returned during G1. A majority of the alkaline phosphatase activity lost from the cell surface at mitosis was recovered in the medium. Tartrate-sensitive acid phos-phatase and non-specific esterase levels were relatively stable throughout the cell cycle, while tartrate-resistant acid phosphatase activity was not assavable at the density used in synchronous cultures. From these data, variations in alkaline phosphatase activity appear to reflect the distribution of cells throughout the cell cycle.

Additional Material: 6 Ill.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1002/jcp.1041440115

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7

Electronic Resource

Fedarko, N. S. ; Vetter, U. K. ; Weinstein, S. ; [et al.]

New York, NY [u.a.] : Wiley-Blackwell

Journal of Cellular Physiology 151 (1992), S. 215-227

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ISSN: 0021-9541

Keywords: Life and Medical Sciences ; Cell & Developmental Biology

Source: Wiley InterScience Backfile Collection 1832-2000

Topics: Biology , Medicine

Notes: Human bone cells grown in culture, representative of a preosteoblastic stage of maturation, produce an extracellular matrix composed of collagen several noncollagenous glycoproteins, hyaluronan, and four distinct proteoglycans (PGs). The influence of donor age on the levels of expression of these molecules in vitro has not been well characterized. In this study, human bone cells derived from sources ranging from fetal to 60-year-old donors were grown in culture, radiolabeled for 24 h, and the amount of incorporation of [35S]sulfate into PGs, [3H]glucosamine into hyaluronan, [3H]leucine/proline into osteonectin, and [3H]proline into collagen was determined. Cell proliferation was most rapid in fetal-derived bone cells and decreased with increasing age. Total protein and PG synthesis also decreased with increasing age, falling to 1/3 and 1/4, respectively, of fetal levels after age 30. A large chondroitin sulfate PG (Mr ∼ 600,000 Da) was the major fetal PG and its levels were highly correlated with cellular proliferation. [3H]Collagen and [35S]decorin levels increased with the increasing age of the donor, reached a maximum in puberty-derived cells, and decreased to 1/3 maximal levels after age 20. The heparan sulfate PG (Mr ∼ 400,000 Da) exhibited steadystate levels regardless of donor age. [3H]Osteonectin and [35S]biglycan levels were high in fetal-derived cells and in cells derived from pubescent donors. The percentage of collagen and four proteoglycans associated with the cell layer pool changed with donor age. All fetal-derived PG core proteins possessed more N- and O-linked oligosaccharides than newborn or adult derived PGs. © 1992 Wiley-Liss, Inc.

Additional Material: 7 Ill.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1002/jcp.1041510202

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