Cloning of apg-2 encoding a novel member of heat shock protein 110 family

Kaneko, Yoshiyuki; Kimura, Toshio; Kishishita, Masamichi; Noda, Yoichi; Fujita, Jun

doi:10.1016/s0378-1119(96)00807-4

Cited by 59 publications

(42 citation statements)

References 11 publications

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“…Our phylogenetic analysis also clustered the C. finmarchicus Hsp70 sequence previously identified by Hansen et al (2008) with human Hsp70-like proteins (Hsp70_14, Hsp70_4) that are known to share low sequence and functional similarity with cytosolic Hsp70 forms (Kaneko et al, 1997;Wan et al, 2004). Therefore, previously reported differences in C. finmarchicus Hsp70 inducibility by stressors (Hansen et al, 2008;Voznesensky et al, 2004) may be attributed, at least in part, to differences in the 'Hsp70' transcripts examined.…”

Section: Discussionmentioning

confidence: 73%

“…1) (Kaneko et al, 1997;Wan et al, 2004). The Hsp90 that we have identified in C. finmarchicus is identical to an EST sequence previously reported by Hansen et al (2007) and it falls into a well-supported clade (100% bootstrap support) with cytosolic (Hsp90A) sequences from other organisms including crustaceans, insects, and human (Fig.…”

Section: Identification Of C Finmarchicus Hsp Genes and Phylogeneticmentioning

confidence: 99%

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Heat shock protein expression during stress and diapause in the marine copepod Calanus finmarchicus

Aruda

Baumgartner

Reitzel

et al. 2011

Journal of Insect Physiology

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Graphical Abstract Research HighlightsWe identified 8 heat shock proteins (3 small Hsps, 4 Hsp70's, Hsp90). Hsp70a (cytosolic clade) and Hsp21, and Hsp22 were induced by handling stress. Hsp70a expression was elevated in shallow, active animals. Hsp22 expression was elevated in deep, diapausing animals. 1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 21 22 23 24 25 26 27 28 29 30 31 32 33 34 35 36 37 38 39 40 41 42 43 44 45 46 47 48 *Research highlights

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Section: Discussionmentioning

confidence: 73%

Section: Identification Of C Finmarchicus Hsp Genes and Phylogeneticmentioning

confidence: 99%

Heat shock protein expression during stress and diapause in the marine copepod Calanus finmarchicus

Aruda

Baumgartner

Reitzel

et al. 2011

Journal of Insect Physiology

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“…Hspa5/BiP is also known to have a chaperone-like activity (Hurtley et al 1989, Flynn et al 1991 at the endoplasmic reticulum (Dierks et al 1993). The other stress proteins, Hspa4/apg-2 (Kaneko et al 1997) and Hsp105 (Yasuda et al 1995), are similar to hsp70RY but their functions are not yet known. Two transcription factors, Atf5 and Egr1, were also activated.…”

Section: Des E2mentioning

confidence: 99%

Similarities and differences in uterine gene expression patterns caused by treatment with physiological and non-physiological estrogens

Watanabe¹,

Suzuki²,

Kobayashi³

et al. 2003

Journal of Molecular Endocrinology

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Administration of physiological and non-physiological estrogens during pregnancy or after birth is known to have adverse effects on the development of the reproductive tract and other organs. Although it is believed that both estrogens have similar effects on gene expression, this view has not been tested systematically. To compare the effects of physiological (estradiol; E2) and non-physiological (diethylstilbestrol; DES) estrogens, we used DNA microarray analysis to examine the uterine gene expression patterns induced by the two estrogens. Although E2 and DES induced many genes to respond in the same way, different groups of genes showed varying levels of maximal activities to each estrogen, resulting in different dose-response patterns. Thus, each estrogen has a distinct effect on uterine gene expression. The genes were classified into clusters according to their dose-responses to the two estrogens. Of the eight clusters, only two correlated well with the uterotropic effect of different doses of E2. One of these clusters contained genes that were upregulated by E2, which included genes encoding several stress proteins and transcription factors. The other cluster contained genes that were downregulated by E2, including genes related to metabolism, transcription and detoxification processes. The expression of these genes in estrogen receptor-deficient mice was not affected by E2 treatment, indicating that these genes are affected by the E2-bound estrogen receptor. Thus, of the many genes that are affected by estrogen, it was suggested that only a small number are directly involved in the uterotropic effects of estrogen treatment.

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“…In adult mouse, Hspa4 mRNA is detected in most tissues, with the highest expression in testis, ovary, and spleen (Kaneko et al 1997). In vitro studies have shown that the expression of Hspa4 is not inducible by heat shock (Nonoguchi et al 1999).…”

Section: Introductionmentioning

confidence: 99%

Heat-shock protein HSPA4 is required for progression of spermatogenesis

Held¹,

Barakat²,

Mohamed³

et al. 2011

Reproduction

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Heat-shock protein 110 (HSP110) family members act as nucleotide exchange factors (NEF) of mammalian and yeast HSP70 chaperones during the ATP hydrolysis cycle. In this study, we describe the expression pattern of murine HSPA4, a member of the HSP110 family, during testis development and the consequence of HSPA4 deficiency on male fertility. HSPA4 is ubiquitously expressed in all the examined tissues. During prenatal and postnatal development of gonad, HSPA4 is expressed in both somatic and germ cells; however, expression was much higher in germ cells of prenatal gonads. Analyses of Hspa4-deficient mice revealed that all homozygous mice on the hybrid C57BL/6J!129/Sv genetic background were apparently healthy. Although HSPA4 is expressed as early as E13.5 in male gonad, a lack of histological differences between Hspa4 K/K and control littermates suggests that Hspa4 deficiency does not impair the gonocytes or their development to spermatogonia. Remarkably, an increased number of the Hspa4-deficient males displayed impaired fertility, whereas females were fertile. The total number of spermatozoa and their motility were drastically reduced in infertile Hspa4-deficient mice compared with wild-type littermates. The majority of pachytene spermatocytes in the juvenile Hspa4 K/K mice failed to complete the first meiotic prophase and became apoptotic. Furthermore, down-regulation of transcription levels of genes known to be expressed in spermatocytes at late stages of prophase I and post-meiotic spermatids leads to suggest that the development of most spermatogenic cells is arrested at late stages of meiotic prophase I. These results provide evidence that HSPA4 is required for normal spermatogenesis.

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Cloning of apg-2 encoding a novel member of heat shock protein 110 family

Cited by 59 publications

References 11 publications

Heat shock protein expression during stress and diapause in the marine copepod Calanus finmarchicus

Heat shock protein expression during stress and diapause in the marine copepod Calanus finmarchicus

Similarities and differences in uterine gene expression patterns caused by treatment with physiological and non-physiological estrogens

Heat-shock protein HSPA4 is required for progression of spermatogenesis

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