Zink (intrazellulär): the pathway in the body

Zink (intrazellulär) is part of the pathway “Zinc”. This page shows the whole pathway; the station of Zink (intrazellulär) is highlighted.

Where this laboratory value sits: Zinc in food — bound to protein. Zinc is found mainly in meat, cheese, nuts, pulses and cereals. It is not free there but bound to proteins and other molecules. Source 4

In brief

Zinc is a trace element found in thousands of proteins. It occupies the active site of enzymes, gives zinc finger proteins their shape, and a tiny free share acts as a signal inside the cell.

The pathway step by step

1. Zinc in food → Free zinc in the gut Digestive enzymes Digestive enzymes break down the proteins and release zinc. Phytate from cereals and pulses binds free zinc ions in the gut contents and holds on to part of them. Source 4, 1
2. Free zinc in the gut → Into the gut cell ZIP4 The ZIP4 transporter sits on the side of the gut cell facing the gut contents and moves zinc into the cell. When little zinc is on offer, the cell inserts more ZIP4. Source 1
3. Into the gut cell → Zinc in the blood ZnT1 On the other side of the gut cell, the transporter ZnT1 releases zinc into the blood. There it is passed on mostly bound to albumin. Source 1, 4
4. Zinc in the blood → Zinc in the cell ZIP transporters Cells bring zinc in via ZIP transporters; ZnT transporters move it into storage compartments or back out. Together, both families keep the amount inside the cell constant. Source 1
5. Free zinc → Metallothionein MTF-1 When free zinc rises, it binds to the switch MTF-1. This attaches to DNA and triggers the formation of metallothionein — a small protein that binds zinc and releases it again as needed. Source 3, 5
6. Free zinc → Zinc enzymes In many enzymes, a zinc ion sits firmly in the active site and holds in position the water molecule that carries out the reaction — for example in carbonic anhydrase or alkaline phosphatase. Source 2
7. Free zinc → Zinc finger proteins In zinc finger proteins, zinc holds a small protein loop in shape. Only then does the loop fit a specific site on the DNA, allowing the cell to read genes there. Source 2, 5

Cofactors in this pathway

• Cysteine — The sulfur of its side chain binds zinc in zinc fingers and in metallothionein Source 6, 7
• Histidine — The nitrogen of its side chain binds zinc in many enzymes and zinc fingers Source 6In the ORY catalogue as a laboratory value: Histidin
• Magnesium — Sits next to two zinc ions in the active site of alkaline phosphatase Source 8In the ORY catalogue as a laboratory value: Magnesium
• Copper — The second metal of superoxide dismutase 1: copper converts, zinc holds the shape Source 9In the ORY catalogue as a laboratory value: Kupfer (Cu)

Sources

1. Kambe T, Tsuji T et al. The Physiological, Biochemical, and Molecular Roles of Zinc Transporters in Zinc Homeostasis and Metabolism. Physiol Rev 2015 · PubMed 26084690
2. Maret W. Zinc biochemistry: from a single zinc enzyme to a key element of life. Adv Nutr 2013 · PubMed 23319127
3. Andrews GK. Cellular zinc sensors: MTF-1 regulation of gene expression. Biometals 2001 · PubMed 11831458
4. Stiles LI, Ferrao K et al. Role of zinc in health and disease. Clin Exp Med 2024 · PubMed 38367035
5. Maret W. Zinc in Cellular Regulation: The Nature and Significance of "Zinc Signals". Int J Mol Sci 2017 · PubMed 29088067
6. Maret W. Zinc coordination environments in proteins determine zinc functions. J Trace Elem Med Biol 2005 · PubMed 16240665
7. Coyle P, Philcox JC, Carey LC et al. Metallothionein: the multipurpose protein. Cell Mol Life Sci 2002 · PubMed 12022471
8. Coleman JE. Structure and mechanism of alkaline phosphatase. Annu Rev Biophys Biomol Struct 1992 · PubMed 1525473
9. Leitch JM, Yick PJ, Culotta VC. The right to choose: multiple pathways for activating copper,zinc superoxide dismutase. J Biol Chem 2009 · PubMed 19586921

Whole pathway: Zinc

Related pathways

• Histamine — Histidin, Kupfer (Cu)
• Dopamine, noradrenaline, adrenaline — Magnesium, Kupfer (Cu)

As of 2026-09-16. Draft, written by Claude to schema v2; sources checked in PubMed; expert approval pending
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