Effects of Interleukin-3 on Murine Fetal Liver Hemopoiesis in utero

Delorme, Danielle; Daniels, Eugene

doi:10.1159/000243890

Cited by 3 publications

(2 citation statements)

References 10 publications

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“…The heterogenous distribution of Timp-3 mRNA in liver suggests that such a phenomenon occurs in discrete regions. During development the different regions of the liver develop asynchronously (Delorme and Daniels, 1992), and our findings may reflect this phenomenon. For example, in response to interleukin-3, the hematopoietic cells of the liver show changes only in restricted regions of the liver, but not throughout its architecture (DeLorme and Daniels, 1992).…”

Section: Timp-3 Expression In the Liver And Kidneysupporting

confidence: 66%

Gene encoding a novel murine tissue inhibitor of metalloproteinases (TIMP), TIMP‐3, is expressed in developing mouse epithelia, cartilage, and muscle, and is located on mouse chromosome 10

Apte

Hayashi

Seldin

et al. 1994

Developmental Dynamics

129

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Remodeling of the extracellular matrix (ECM) is an essential component of normal development and is also involved in the pathogenesis of arthritis and the spread of cancer. The matrix metalloproteinases and their natural inhibitors, the tissue inhibitors of metalloproteinases (TIMPs), play an important role in this context. We have isolated mouse cDNA clones encoding a novel member of the TIMP family, designated TIMP-3. We have assigned the Timp-3 locus to the [Cl-D11 region of mouse chromosome 10 using both genetic and cytogenetic methods. The conceptual translation product of the Timp-3 cDNA shows a high degree of similarity with ChIMP-3, a recently cloned chicken metalloproteinase inhibitor, as well as significant structural similarity with the amino acid sequences of the previously isolated members of this family, TIMP-1 and TIMP-2. The pattern of expression of Timp-3 in the developing mouse embryo is distinct from that previously reported for Timp-1. Timp-3 is expressed in cartilage and skeletal muscle, in myocardium, in the skin, oral and nasal epithelium, in the newborn mouse liver, in the epithelium of some tubular structures such as the developing bronchial tree, oesophagus, colon, urogenital sinus, bile duct, in the kidney, salivary glands, and in the choroid plexus of the brain. The patterns of Timp-3 expression in surface epithelia and in the epithelial lining of many tubular organs suggests that TIMP-3 may be involved in regulating ECM remodeling during the folding of epithelia and during the formation, branching, and expansion of epithelial tubes. In the mouse placenta, expression is seen in the trophoblast, raising the possibility that TIMP-3 may be involved in regulating trophoblastic invasion of the uterus. We propose a role for TIMP-3 in musculoskeletal and cardiac development, in the morphogenesis of certain epithelial structures, and placental implantation.

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Section: Timp-3 Expression In the Liver And Kidneysupporting

confidence: 66%

Gene encoding a novel murine tissue inhibitor of metalloproteinases (TIMP), TIMP‐3, is expressed in developing mouse epithelia, cartilage, and muscle, and is located on mouse chromosome 10

Apte

Hayashi

Seldin

et al. 1994

Developmental Dynamics

129

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“…The NIL-3 activity of fractionated sample at each step is indicated below (b). genitors (Delorme and Daniels, 1992;Spivak et al, 1985). Especially in hematopoietic progenitors, IL-3 stimulates the proliferation and/or differentiation together with lineage specific cytokines such as Epo, G-, M-, and GM-CSF.…”

Section: Discussionmentioning

confidence: 99%

Identification of Negative Regulator of Interleukin-3 (NIL-3) in Bone Marrow.

Adachi

Sugimoto²,

Sato³

et al. 2002

Cell Struct. Funct.

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ABSTRACT. We have reported that an inhibitor of interleukin-3 (NIL-3) is produced from murine bone marrow cells in response to excess stimulation of interleukin-3. In this report, we attempted the purification of the NIL-3 activity from bone marrow culture supernatant in the presence of interleukin-3. The purified NIL-3 activity was a protein with relative molecular weight of 54.5 kDa (SDS-PAGE), which inhibited the growth of IL-3 dependent DA-1 cell growth in a dose dependent manner. The N-terminal amino acid sequence of purified NIL-3 activity was determined to be homologous to beta-2 glycoprotein I (apolipoprotein H: APO-H). The gene expression of APO-H was detected by nested-PCR in STIL-3 C5-CM stimulated total bone marrow cells and STIL-3 C5-CM stimulated bone marrow fraction 2 (Fr. 2) which has been reported as a hematopoietic stem cell rich fraction. These observations indicate the possibility that the APO-H is the NIL-3 which was produced from bone marrow cells in response to excess IL-3 stimuli.

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