Evidence map›Paper›PMID 15967430›Full record

ArticleExperimental eye research2005

Serca isoform expression in the mammalian retina.

David Krizaj

Open access · greenAbstract read
In one paragraph

Article in Experimental eye research, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
0.8field-weighted citation impact, top 30% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

17 citing papers in PubMed, 24 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Glycine Release Is Potentiated by cAMP via EPAC2 and CaThe Journal of neuroscience : the official journal of the Society for Neuroscience · 2021
    Article
  8. Article
  9. Endoplasmic reticulum (ER) CaThe Journal of biological chemistry · 2017
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Calcium stores in vertebrate photoreceptors.Advances in experimental medicine and biology · 2012
    Review
  15. Review
  16. Article
  17. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

1 author at 1 institution in 1 country.

David KrizajDept. of Ophthalmology, Beckman Vision Center, UCSF School of Medicine, Rm. K-140, 10 Kirkham St., San Francisco, CA 94143-0730, USA. krizaj@phy.ucsf.edu
University of California, San Francisco · US

Funding

REGULATION OF NEUROTRANSMISSION IN THE RETINAR01EY013870 · NEI · UNIVERSITY OF UTAH · PI KRIZAJ, DAVID · 2002 to 2011
$2.7M
NEI NIH HHS EY13870NEI NIH HHS R01 EY013870
6 · The paper itself

Abstract

The sarcoplasmic-endoplasmic reticulum calcium ATPase (SERCA) is a key intracellular calcium transporter, which regulates cellular calcium concentration [Ca2+] by transporting Ca2+ ions from the cytosol into the endoplasmic reticulum. SERCA-mediated Ca2+ sequestration controls proper folding of newly synthesized proteins within the ER as well as the timing and spatial patterning of depolarization-evoked Ca2+ responses in the cytoplasm. To understand the spatial and temporal properties of Ca2+ homeostasis in retinal neurons better, I studied expression and distribution of all three SERCA isoforms in the mouse retina using isoform-specific antibodies. No immunostaining was observed with the SERCA1 antibody. SERCA2 was expressed in photoreceptor inner segments, amacrine and ganglion cells of the mouse retina. Similar SERCA2 localization was observed in adult rat, macaque and ground squirrel retinas. Analysis of distribution of SERCA2 immunofluorescence in the developing mouse retina revealed prominent SERCA2 signals throughout postnatal development. The N89 antibodys used to identify the SERCA3 isoforms labelled cone outer segments, inner segments of photoreceptors and cell processes in the inner nuclear layer of the mouse retina. These results imply that the SERCA2 isoform controls Ca2+ sequestration into the endoplasmic reticulum in most classes of retinal neuron. A potential role for SERCA3 in cone function is suggested.

Indexed as

AnimalsBiological TransportCalciumCalcium-Transporting ATPasesEndoplasmic ReticulumIsoenzymesMacacaMiceMice, Inbred BALB CMice, Inbred C57BLMice, Inbred CBAMicroscopy, ConfocalMicroscopy, ImmunoelectronPhotoreceptor Cells, VertebrateRatsRats, Long-EvansAtp2a1 protein, mouseAtp2a1 protein, ratAtp2a2 protein, mouseAtp2a2 protein, ratAtp2a3 protein, mouseAtp2a3 protein, ratCalciumCalcium-Transporting ATPasesIsoenzymesSarcoplasmic Reticulum Calcium-Transporting ATPases

Identifiers

PMID15967430
PMCPMC2921800
OpenAlexW2095037040

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.