1983
DOI: 10.1016/0014-5793(83)80370-6
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On the presence of two new high mobility group‐like proteins in HeLa S3 cells

Abstract: Two phosphorylated HMG-like proteins with M, -10 000 have been isolated from HeLa S3 cells, one being present in metaphase and one in interphase cells. The amino acid compositions of these proteins are very similar but differ from the known HMG proteins. However, they exhibit similarities being rich in proline, basic and acidic amino acids. A possible role in chromatin condensation of the HMG-like protein characteristic for metaphase cells is suggested.High mobility group-like protein Interphase Metaphase Phos… Show more

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Cited by 150 publications
(117 citation statements)
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“…PSA was measured periodically (once per 6 months) during the follow-up of the (Figure 3 log-rank test: chi-square = 5.0175, P= 0.025). Increased HMG-I(Y) mRNA levels are often found in rapidly proliferating or undifferentiated cells and in various malignant tissues including prostate cancer (Lund et al, 1983;Elton et al, 1986;Johnson et al, 1988;Bussemakers et al, 1991). Furthermore, induction of differentiation results in the down-regulation of HMG-I(Y) mRNA expression, suggesting that HMG-I(Y) expression is associated with cellular differentiation (Vartianen et al, 1988).…”
Section: Psa Levels and Hmg-i(y) Expression Correlationmentioning
confidence: 99%
“…PSA was measured periodically (once per 6 months) during the follow-up of the (Figure 3 log-rank test: chi-square = 5.0175, P= 0.025). Increased HMG-I(Y) mRNA levels are often found in rapidly proliferating or undifferentiated cells and in various malignant tissues including prostate cancer (Lund et al, 1983;Elton et al, 1986;Johnson et al, 1988;Bussemakers et al, 1991). Furthermore, induction of differentiation results in the down-regulation of HMG-I(Y) mRNA expression, suggesting that HMG-I(Y) expression is associated with cellular differentiation (Vartianen et al, 1988).…”
Section: Psa Levels and Hmg-i(y) Expression Correlationmentioning
confidence: 99%
“…Such stimuli affect HMGA1 activity, in part, by altering their pattern of post-translational modifications which results in changes to the proteins ability to interact with different DNA and protein substrates [2,3,4]. Because of their small size (10.6-12 kDa) [5], inherent flexibility [6], and high levels of post-translational modifications, the proteins are uniquely equipped to adapt and function in a highly regulated manner. Additionally, HMGA1 proteins are unified by their possession of a versatile DNA binding motif called the AT-hook [7].…”
Section: Introductionmentioning
confidence: 99%
“…Although HMG-I/Y expression is increased in a variety of human cancers and portends a poor prognosis in some tumors (1)(2)(3)(4), the contribution of this gene to malignant transformation is unknown. The HMG-I/Y gene encodes the HMG-I and HMG-Y protein isoforms (1)(2)(3), which function as architectural chromatin-binding proteins involved in regulating gene expression (1)(2)(3)(5)(6)(7)(8).…”
Section: Introductionmentioning
confidence: 99%
“…The HMG-I/Y gene encodes the HMG-I and HMG-Y protein isoforms (1)(2)(3), which function as architectural chromatin-binding proteins involved in regulating gene expression (1)(2)(3)(5)(6)(7)(8). Interestingly, this gene is located on the short arm of chromosome 6, in a region known to be involved in rearrangements, translocations, and other abnormalities correlated with human cancers (1)(2)(3). We showed previously (9) that HMG-I/Y is a c-Myc target gene involved in Burkitt's lymphoma, an aggressive childhood malignancy that develops as a consequence of deregulated c-myc expression.…”
Section: Introductionmentioning
confidence: 99%