The multifaceted roles of neutrophil gelatinase associated lipocalin (NGAL) in inflammation and cancer
Open accessAbstract
Neutrophil gelatinase associated lipocalin (NGAL), also known as oncogene 24p3, uterocalin, siderocalin or lipocalin 2, is a 24kDa secreted glycoprotein originally purified from a culture of mouse kidney cells infected with simian virus 40 (SV-40). Subsequent investigations have revealed that it is a member of the lipocalin family of proteins that transport small, hydrophobic ligands. Since then, NGAL expression has been reported in several normal tissues where it serves to provide protection against bacterial infection and modulate oxidative stress. Its expression is also dysregulated in several benign and malignant diseases. Its small size, secreted nature and relative stability have led to it being investigated as a diagnostic and prognostic biomarker in numerous diseases including inflammation and cancer. Functional studies, conducted primarily on lipocalin 2 (Lcn2), the mouse homologue of human NGAL have revealed that Lcn2 has a strong affinity for iron complexed to both bacterial siderophores (iron-binding proteins) and certain human proteins like norepinephrine. By sequestering iron-laden siderophores, Lcn2 deprives bacteria of a vital nutrient and thus inhibits their growth (bacteriostatic effect). In malignant cells, its proposed functions range from inhibiting apoptosis (in thyroid cancer cells), invasion and angiogenesis (in pancreatic cancer) to increasing proliferation and metastasis (in breast and colon cancer). Ectopic expression of Lcn2 also promotes BCR-ABL induced chronic myelogenous leukemia in murine models. By transporting iron into and out of the cell, NGAL also regulates iron responsive genes. Further, it stabilizes the proteolytic enzyme matrix metalloprotease-9 (MMP-9) by forming a complex with it, and thereby prevents its autodegradation. The factors regulating NGAL expression are numerous and range from pro-inflammatory cytokines like interleukins, tumor necrosis factor-α and interferons to vitamins like retinoic acid. The purpose of this review article is to examine the expression, structure, regulation and biological role of NGAL and critically assess its potential as a novel diagnostic and prognostic marker in both benign and malignant human diseases.
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Siderophores are synthesized and secreted by bacteria into their microenvironment to acquire soluble iron or to steal the metal from host iron proteins.
“Siderophores are synthesized and secreted by bacteria into their microenvironment to acquire soluble iron or to steal the metal from host iron proteins (205).”
From Macrophage defense mechanisms against intracellular bacteria (2015) · cites this paper as [205]
Lcn2 is an anti-microbial peptide that exerts its effect upon binding of bacterial siderophores.
“Lcn2 is an anti-microbial peptide which exerts its effect upon binding of bacterial siderophores.”
From Macrophage defense mechanisms against intracellular bacteria (2015) · cites this paper as [205]
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- Authors
- Chakraborty, S., Kaur, S., Guha, S., & Batra, S. K.
- Affiliations
- University of Nebraska Medical Center (US)
- The University of Texas MD Anderson Cancer Center (US)
- Corresponding author
- Batra, Surinder K.
- Venue
- Biochimica et Biophysica Acta (BBA) - Reviews on Cancer
- Publisher
- Elsevier BV
- Published
- 2012-08
- Volume
- 1826
- Issue
- 1
- Pages
- 129-169
- ISSN
- 0304-419X (ISSN-L)
- PMC
- PMC3362670
- OpenAlex
- W2043806528
- Cited by
- 503
- References
- 277
- Citations by year
- 2026: 7 · 2025: 16 · 2024: 38 · 2023: 34 · 2022: 36 · 2021: 46 · 2020: 50 · 2019: 41 · 2018: 27 · 2017: 38 · 2016: 42 · 2015: 39 · 2014: 52 · 2013: 32 · 2012: 5
- FWCI
- 3.73
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Locations
- Biochimica et Biophysica Acta (BBA) - Reviews on Cancer (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Cancer Institute (R03CA139285, U54CA163120, R01CA133774, P50CA127297, R01 CA139285, U01CA111294, R01 CA78590), R01CA078590, R01CA131944)
- National Institute of Diabetes and Digestive and Kidney Diseases (2P30DK56338, P30DK056338)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › S100 Proteins and Annexins
- Health Sciences › Medicine › Oncology › Chemokine receptors and signaling
- Life Sciences › Immunology and Microbiology › Immunology › Neutrophil, Myeloperoxidase and Oxidative Mechanisms
- Keywords
- neutrophil gelatinase-associated lipocalin, inflammation, cancer, iron metabolism, bacterial infection, MMP-9, angiogenesis, metastasis, apoptosis, chronic myeloid leukemia, BCR-ABL, prognostic factors, diagnostic biomarkers, cytokine regulation, retinoic acid
- MeSH terms
- Lipocalin-2, Acute-Phase Proteins, Animals, Humans, Inflammation, Neoplasms, Proto-Oncogene Proteins, Oncogene Proteins, Lipocalins
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