Evidence map›Paper›PMID 15469915›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2004

Development of a polyclonal antiserum for the detection of the isoforms of the receptors for human growth hormone-releasing hormone on tumors.

Gabor L Toller, Judit E Horvath, Andrew V Schally, Gabor Halmos, Jozsef L Varga, Kate Groot, David Chism, Marta Zarandi

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
2.3field-weighted citation impact, top 11% 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

9 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
  2. Acceleration of wound healing by growth hormone-releasing hormone and its agonists.Proceedings of the National Academy of Sciences of the United States of America · 2010
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Effective treatment of experimental human non-Hodgkin's lymphomas with antagonists of growth hormone-releasing hormone.Proceedings of the National Academy of Sciences of the United States of America · 2005
    Article
  8. Article
  9. 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

8 authors at 1 institution in 1 country.

Gabor L TollerEndocrine, Polypeptide, and Cancer Institute, Veterans Affairs Medical Center, New Orleans, LA 70112-1262, USA.
Judit E Horvath
Andrew V Schally
Gabor Halmos
Jozsef L Varga
Kate Groot
David Chism
Marta Zarandi
Tulane University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Antagonists of growth hormone-releasing hormone (GHRH) inhibit the growth of various human cancers by multiple mechanisms, which include direct effects on tumor cells through the splice variants (SV) of the GHRH receptor. Our findings suggest that the tumoral protein encoded by SV 1 (SV1) is a likely functional receptor. The aim of this study was to develop a polyclonal antiserum against a polypeptide analog of segment 1-25 of the putative SV1 receptor protein. Rabbits were immunized with [Ala-23]SV1 (1-25)-Tyr-26-Cys-27-NH2 as a hapten, conjugated to BSA or keyhole limpet hemocyanin. The antisera thus generated were evaluated by RIA for binding to the radiolabeled hapten. The specificity and sensitivity of the antisera were studied on xenografts of RL and HT human non-Hodgkin's lymphomas. The sera raised against keyhole limpet hemocyanin-SV1 hapten, showed binding values of 50-75% at a 1:56,000 dilution. In Western blot analyses, the purified polyclonal antibody recognized a specific signal with a molecular mass of approximately 40 kDa in RL and HT lymphomas. This band corresponds to the estimated molecular mass of the GHRH receptor isoform encoded by SV1. RT-PCR and ligand binding studies also revealed the expression of SV1 and the presence of high-affinity binding sites for GHRH on RL and HT tumors. Because the antiserum developed recognizes the tumoral GHRH receptor protein encoded by SV1, it should be of value in various investigations.

Indexed as

AnimalsAntibodiesCell Line, TumorFemaleGenetic VariationHumansLymphoma, Non-HodgkinMiceMice, NudeNeoplasmsProtein IsoformsRabbitsReceptors, NeuropeptideReceptors, Pituitary Hormone-Regulating HormoneTransplantation, HeterologousAntibodiesProtein IsoformsReceptors, NeuropeptideReceptors, Pituitary Hormone-Regulating Hormonesomatotropin releasing hormone receptor

Identifiers

PMID15469915
PMCPMC524040
OpenAlexW2149123380

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.