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Related Concept Videos

Chemical Signaling in the Endocrine System01:08

Chemical Signaling in the Endocrine System

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A signaling cascade is a series of events that facilitates the transmission of information within or between cells, culminating in a targeted response in the recipient cell. As chemical messengers, hormones are pivotal in initiating and modulating these intricate signaling cascades based on their solubility.
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Endocrine Signaling01:45

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Endocrine cells produce hormones to communicate with remote target cells found in other organs. The hormone reaches these distant areas using the circulatory system. This exposes the whole organism to the hormone but only those cells expressing hormone receptors or target cells are affected. Thus, endocrine signaling induces slow responses from its target cells but these effects also last longer.
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Related Experiment Video

Updated: Mar 31, 2026

Evaluation of Tumor-infiltrating Leukocyte Subsets in a Subcutaneous Tumor Model
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Decoding chemerin proteolytic processing and isoform signaling across disease contexts.

Jing Wang1,2, Jiangming Deng1,2, Ting Xiao2,3

  • 1National Clinical Research Center for Endocrine and Metabolic Diseases and Metabolism and Endocrinology, The Second Xiangya Hospital of Central South University, Changsha, Hunan 410011, China.

Iscience
|March 30, 2026
PubMed
Summary
This summary is machine-generated.

Chemerin (RARRES2) signaling is complex due to its processing into various isoforms. Understanding these specific chemerin proteoforms and their locations is crucial for accurate clinical interpretation and targeted therapies.

Keywords:
health sciences

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Endocrinology

Background:

  • Chemerin (RARRES2) is a key adipokine involved in metabolic, inflammatory, cardiovascular, and neoplastic diseases.
  • Current clinical interpretations of chemerin are limited by measuring total levels, masking crucial proteoform-specific signaling.
  • Chemerin is secreted as an inactive precursor and processed into active isoforms with varying receptor affinities and tissue distribution.

Purpose of the Study:

  • To decode the functional duality of chemerin by examining its isoform processing and receptor interactions.
  • To establish a framework for interpreting chemerin's role in disease by considering its specific proteoforms and localization.
  • To highlight methods for isoform-resolved quantification and potential therapeutic targeting strategies.

Main Methods:

  • Review of existing literature on chemerin processing, bioactivity, and receptor interactions (CMKLR1, GPR1, CCRL2).
  • Emphasis on targeted/MRM-MS for isoform-specific quantification.
  • Development of a compartment-aware framework for clinical data interpretation.

Main Results:

  • Chemerin bioactivity is determined by protease-encoded isoform "barcodes."
  • Distinct isoform landscapes exist in human biofluids and disease microenvironments.
  • Receptor context (CMKLR1, GPR1, CCRL2) modulates chemerin signaling output.

Conclusions:

  • Measuring total chemerin is mechanistically misleading; isoform-specific analysis is essential.
  • A compartment-aware framework improves the interpretation of complex disease associations linked to chemerin.
  • Isoform-resolved quantification and understanding localization offer new avenues for targeted therapeutic interventions.